研究者業績

柴田 直樹

シバタ ナオキ  (Naoki Shibata)

基本情報

所属
兵庫県立大学 大学院理学研究科生命科学専攻 助教授・准教授
学位
博士(工学)(大阪大学)

J-GLOBAL ID
200901039667162990
researchmap会員ID
1000224235

外部リンク

論文

 138
  • K.Suto, N.Shibata, Y.Morimoto, N.Yasuoka
    J.Phys.Soc.Jpn.\n 70 406-407 2001年  査読有り
  • K Uemura, N Shibata, Anwaruzzaman, M Fujiwara, T Higuchi, H Kobayashi, Y Kai, A Yokota
    JOURNAL OF BIOCHEMISTRY 128(4) 591-599 2000年10月  査読有り
    Many enzymes are composed of subunits with the identical primary structure. It has been believed that the protein structure of these subunits is the same. Ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO) comprises eight large subunits with the identical amino acid sequence and eight small subunits. Rotation of the side chains of the lysine residues, Lys-21 and Lys-305, in each of the eight large subunits in spinach RuBisCO in two ways produces microheterogeneity among the subunits. These structures are stabilized through hydrogen bonds by water molecules incorporated into the large subunits. This may cause different effects upon catalysis and a hysteretic, time-dependent decrease in activity in spinach RuBisCO, Changing the amino acid residues corresponding to Lys-21 and Lys-305 in non-hysteretic Chromatium vinosum RuBisCO to lysine induces hysteresis and increases the catalytic activity from 8.8 to 15.8 per site per second. This rate is approximately five times higher than that of the higher-plant enzyme.
  • 柴田 直樹, 安岡 則武
    日本結晶学会誌 42(4) 354-360 2000年8月31日  査読有り筆頭著者
    Diol dehydratase is an adenosylcobalamin-dependant enzyme that catalyzes conversion from 1, 2-diol compounds to corresponding aldehydes. The crystal structure of the enzyme shows that B12 compounds are incorporated with the DBI-on mode. The enzyme has a potassium ion at the active site, where the substrate coordinates to it. The structure of the enzyme complexed with adeninylpentylcobalamin reveals the activation mechanism of adenosylcobalamin.
  • J Masuda, N Shibata, Y Morimoto, T Toraya, N Yasuoka
    STRUCTURE WITH FOLDING & DESIGN 8(7) 775-788 2000年7月  査読有り
    Background: Adenosylcobalamin (coenzyme B-12) serves as a cofactor for enzymatic radical reactions. The adenosyl radical, a catalytic radical in these reactions, is formed by homolysis of the cobalt-carbon bond of the coenzyme, although the mechanism of cleavage of its organometallic bond remains unsolved. Results: We determined the three-dimensional structures of diet dehydratase complexed with adeninylpentylcobalamin and with cyanocobalamin at 1.7 Angstrom and 1.9 Angstrom resolution, respectively, at cryogenic temperatures. In the adeninylpentylcobalamin complex, the adenine ring is bound parallel to the corrin ring as in the free form and methylmalonyl-CoA-mutase-bound coenzyme, but with the other side facing pyrrole ring C. All of its nitrogen atoms except for N(9) are hydrogen-bonded to mainchain amide oxygen and amide nitrogen atoms, a sidechain hydroxyl group, and a water molecule. As compared with the cyanocobalamin complex, the sidechain of Ser alpha 224 rotates by 120 degrees to hydrogen bond with N(3) of the adenine ring. Conclusions: The structure of the adenine-ring-binding site provides a molecular basis for the strict specificity of diol dehydratase for the coenzyme adenosyl group. The superimposition of the structure of the free coenzyme on that of enzyme-bound adeninylpentylcobalamin demonstrated that the tight enzyme-coenzyme interactions at both the cobalamin moiety and adenine ring of the adenosyl group would inevitably lead to cleavage of the cobalt-carbon bond. Rotation of the ribose moiety around the glycosidic linkage makes the 5'-carbon radical accessible to the hydrogen atom of the substrate to be abstracted.
  • K Suto, K Kawagoe, N Shibata, Y Morimoto, Y Higuchi, M Kitamura, T Nakaya, N Yasuoka
    ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY 56 368-371 2000年3月  査読有り
    The crystal structure of FMN-binding protein (FMN-bp) from Desulfovibrio vulgaris Miyazaki F was solved by the multiple isomorphous replacement method and refined to an Ii: factor of 15.1% at 1.3 Angstrom resolution. FMN-bp exists in a dimeric form in the crystal, in contrast to the monomeric structure determined by NMR. R.m.s. deviations between the crystal structure and the solution structure are more than 2 Angstrom, which implies significant differences, There are some hydrophobic residues in the interface between the two monomers. In particular, Leu122 in the C-terminus has a close contact with the o-xylene moiety of FMN, while solvent molecules may cover the o-xylene moiety in the solution structure.
  • T Matsumoto, Y Morimoto, N Shibata, T Kinebuchi, N Shimamoto, T Tsukihara, N Yasuoka
    JOURNAL OF BIOCHEMISTRY 127(2) 329-335 2000年2月  査読有り
    The single-stranded DNA (ssDNA) binding protein from Escherichia coli (EcoSSB) plays a central role in DNA replication, recombination, and repair: The tertiary structure of EcoSSB was determined at 2.2 Angstrom resolution. This is rather higher resolution than previously reported. Crystals were grown from the homogeneous intact protein but the EcoSSB tetramer in the crystals contains truncated subunits lacking a part of the C-terminal, The structure determined includes biologically important flexible loops and C-terminal regions, and revealed the existence of concavities. These concavities include the residues important for ssDNA binding. An ssDNA can be fitted on the concavities and further stabilized through interactions with the loops forming flexible lids. It seems likely to play a central role in the binding of ssDNA.
  • 須藤 恭子, 柴田 直樹, 森本 幸生, 樋口 芳樹, 安岡 則武
    生物物理 40 S121 2000年  
  • N.Shibata, J.Masuda, Y.Morimoto, N.Yasuoka
    SPring-8 User Experiment Report 4 182 2000年  筆頭著者
  • K.Satoh, Y.Yano, H.Koike, N.Shibata, Y.Morimoto, N.Yasuoka
    SPring-8 User Experiment Report 4 190 2000年  
  • N.Shibata, J.Masuda, Y.Morimoto, N.Yasuoka
    SPring-8 User Experiment Report 5 297 2000年  筆頭著者
  • N.Shibata, K.Suto, Y.Morimoto, N.Yasuoka
    SPring-8 User Experiment Report 4 181 2000年  筆頭著者
  • Y.Morimoto, K.Sudo, N.Shibata, N.Yasuoka
    SPring-8 User Experiment Report 5 455 2000年  
  • N Shibata, J Masuda, T Tobimatsu, T Toraya, K Suto, Y Morimoto, N Yasuoka
    STRUCTURE WITH FOLDING & DESIGN 7(8) 997-1008 1999年8月  査読有り筆頭著者
    Background: Diol dehydratase is an enzyme that catalyzes the adenosylcabalamin (coenzyme B-12) dependent conversion of 1,2-diols to the corresponding aldehydes, The reaction initiated by homolytic cleavage of the cobalt-carbon bond of the coenzyme proceeds by a radical mechanism. The enzyme is an alpha(2)beta(2)gamma(2) heterooligomer and has an absolute requirement for a potassium ion for catalytic activity. The crystal structure analysis of a diol dehydratase-cyanocobalamin complex was carried out in order to help understand the mechanism of action of this enzyme. Results: The three-dimensional structure of diet dehydratase in complex with cyanocobalamin was determined at 2.2 Angstrom resolution. The enzyme exists as a dimer of heterotrimers (alpha beta gamma)(2) The cobalamin molecule is bound between the alpha and beta subunits in the 'base-on' mode, that is, 5,6-dimethylbenzimidazole of the nucleotide moiety coordinates to the cobalt atom in the lower axial position. The alpha subunit includes a (beta/alpha)(8) barrel, The substrate, 1,2-propanediol, and an essential potassium ion are deeply buried inside the barrel. The two hydroxyl groups of the substrate coordinate directly to the potassium ion. Conclusions: This is the first crystallographic indication of the 'base-on' mode of cobalamin binding. An unusually long cobalt-base bond seems to favor homolytic cleavage of the cobalt-carbon bond and therefore to favor radical enzyme catalysis. Reactive radical intermediates can be protected from side reactions by spatial isolation inside the barrel. On the basis of unique direct interactions between the potassium ion and the two hydroxyl groups of the substrate, direct participation of a potassium ion in enzyme catalysis is strongly suggested.
  • H Sugawara, H Yamamoto, N Shihata, T Inoue, S Okada, C Miyake, A Yokota, Y Kai
    JOURNAL OF BIOLOGICAL CHEMISTRY 274(22) 15655-15661 1999年5月  査読有り
    Ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco, EC 4.1.1.39) obtained from a thermophilic red alga Galdieria partita has the highest specificity factor of 238 among the Rubiscos hitherto reported. Crystal structure of activated Rubisco from G. partita complexed with the reaction intermediate analogue, 2-carboxyarabinitol 1,5-bisphosphate (P-CABP) has been determined at 2.4-Angstrom resolution. Compared with other Rubiscos, different amino residues bring the structural differences in active site, which are marked around the binding sites of P-2 phosphate of 2-CABP. Especially, side chains of His-327 and Arg-295 show the significant differences from those of spinach Rubisco. Moreover, the side chains of Asn-123 and His-294 which are reported to bind the substrate, ribulose 1,5-bisphosphate, form hydrogen bonds characteristic of Galdieria Rubisco. Small subunits of Galdieria Rubisco have more than 30 extra amino acid residues on the C terminus, which make up a hairpin-loop structure to form many interactions with the neighboring small subunits. When the structures of Galdieria and spinach Rubiscos are superimposed, the hairpin region of the neighboring small subunit in Galdieria enzyme and apical portion of insertion residues 52-63 characteristic of small subunits in higher plant enzymes are almost overlapped to each other.
  • K Suto, K Kawagoe, N Shibata, Y Morimoto, Y Higuchi, M Kitamura, T Nakaya, N Yasuoka
    ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY 55 1089-1090 1999年5月  査読有り
    The flavin mononucleotide binding protein from Desulfovibrio vulgaris (Miyazaki F) was crystallized using the vapour-diffusion method. The crystal belongs to the monoclinic space group P2(1) with unit-cell parameters a = 37.2, b = 84.6, c = 41.1 Angstrom, beta = 94.1 degrees, contains two molecules per asymmetric unit and diffracts beyond 1.2 Angstrom resolution with a synchrotron radiation X-ray source.
  • J Masuda, T Yamaguchi, T Tobimatsu, T Toraya, K Suto, N Shibata, Y Morimoto, Y Higuchi, N Yasuoka
    ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY 55 907-909 1999年4月  査読有り
    Two crystal forms of Klebsiella oxytoca diol dehydratase complexed with cyanocobalamin have been obtained and preliminary crystallographic experiments have been performed. The crystals belong to two different space groups, depending on the crystallization conditions. One crystal (form I) belongs to space group P2(1)2(1)2(1) with unit-cell parameters a = 76.2, b = 122.3, c = 209.6 Angstrom, and diffracts to 2.2 Angstrom resolution using an X-ray beam from a synchrotron radiation source. The other crystal (form II) belongs to space group P2(1) with unit-cell parameters a = 75.4, b = 132.7, c = 298.8 Angstrom, beta = 91.9 degrees, and diffracts to 3.0 Angstrom resolution. For the purpose of structure determination, a heavy-atom derivative search was carried out and some mercuric derivatives were found to be promising. Structure analysis by the multiple isomorphous replacement method is now under way.
  • SHIBATA N, INOUE T, NAGANO C, NISHIO N, KOHZUMA T, ONODERA K, YOSHIZAKI F, SUGIMURA Y, KAI Y
    JOURNAL OF BIOLOGICAL CHEMISTRY 274(7) 4225-4230 1999年2月  査読有り筆頭著者
  • 西尾 和也, 森本 幸生, 柴田 直樹, 小笠原 京子, 油谷 克英, 安岡 則武
    生物物理 39 S117 1999年  
  • 宮崎 忠嗣, 森本 幸生, 柴田 直樹, 小宮 徹, 坂口 雅郎, 三原 勝芳, 安岡 則武
    生物物理 39 S117 1999年  
  • Y Sasakawa, K Onodera, M Karasawa, SC Im, E Suzuki, F Yoshizaki, Y Sugimura, N Shibata, T Inoue, Y Kai, S Nagatomo, T Kitagawa, T Kohzuma
    INORGANICA CHIMICA ACTA 283(1) 184-192 1998年12月  査読有り
    A novel plastocyanin from the green alga Ulva pertusa was isolated and characterized. The electronic absorption and the electron paramagnetic resonance spectroscopic properties of Ulva plastocyanin showed features characteristic of the usual plastocyanins reported so far. However, the resonance Raman spectrum on excitation at 607 nm indicated the Raman band of CuSCys at 413 cm(-1); this is at a lower frequency than the corresponding Raman band of higher plant plastocyanins. Electron-transfer reactions were investigated with [Fe(CN)(6)](3-) and [Co(phen)(3)](3+) complexes. The electron-transfer rate constant of Ulva plastocyanin was determined to be (1.18 +/- 0.06) x 10(5) M-1 s(-1) for the reaction with [Fe(CN)(6)](3-) at pH 7.5, and the intramolecular electron-transfer rate constant and equilibrium constant for complex formation for the reaction with [Co(phen)(3)](3+) were evaluated to be 7.7 +/- 0.6 s(-1) and (4.2 +/- 0.4) x 10(2) M-1 respectively. The electron-transfer rate constant for the reaction with [Fe(CN)(6)](3-) at pH 7.5 is two times larger than the values obtained from the other higher plant plastocyanins. The kinetic behavior suggested that the structure is slightly different from those of other plastocyanins. It has been reported that the electron-transfer reaction of plastocyanin is inhibited by the protonation of the active site histidine (His87 in poplar plastocyanin) at acidic pH. The dependence on pH of the rate constant for the reaction with [Fe(CN)(6)](3-) was investigated. The acid-dissociation constant accompanying the electron-transfer reaction was determined to be pK(H) = 5.8. Second-order rate constants for the reduction of plastocyanin by cytochrome c were determined to be (1.71 +/- 0.04) x 10(6) M-1 s(-1) at I = 0.1 M (NaCl), pH 7.0 (20 mM Tris-HCl buffer). The saturation kinetic behavior for the reaction was not observed even at the lower ionic strength (20 mM Tris-HCl). (C) 1998 Elsevier Science S.A. All rights reserved.
  • N Shibata, S Iba, S Misaki, TE Meyer, RG Bartsch, MA Cusanovich, Y Morimoto, Y Higuchi, N Yasuoka
    JOURNAL OF MOLECULAR BIOLOGY 284(3) 751-760 1998年12月  査読有り筆頭著者
    The crystal structure of an unusual monomeric cytochrome c' from Rhodopseudomonas palustris (RPCP) has been determined at 2.3 Angstrom resolution. RPCP has the four-helix (helices A, B, C and D) bundle structure similar to dimeric cytochromes c'. Ho ct ever the amino acid composition of the surface of helices A and B in RPCP is remarkably different from that of the dimeric cytochromes c'. This surface forms the dimer interface in the latter proteins. RPCP has seven charged residues on this surface contrary to the dimeric cytochromes c', which have only two or three on the corresponding surface. Moreover, hydrophobic charged groups residues on this surface of RTCP are two to three times fewer than in dimeric cytochromes c'. As a result of the difference in amino acid composition, the A-B surface of RTCP is rather hydrophilic compared with dimeric cytochromes c'. We thus suggest that RPCP is monomeric in solution because of the hydrophilic nature of the A-B surface. The amino acid composition of the A-B surface is similar to that of Rhodobacter capsulatus cytochrome c' (RCCP), which is an equilibrium admixture of monomer and dimer. The charge distribution of the A-B surface in RCCP, however, is considerably different from that of RPCP. Due to the difference, RCCP can form dimers by both ionic and hydrophobic interactions. These dimers are quite different h-om those in proteins which form strong dimers such as in Chromatium vinosum, Rhodospirillum rubrum, Rhodospirillum molischianum and Alcaligenes. Cytochrome c' can be classified into two types. Type 1 cytochromes c' have hydrophobic A-B surfaces and they are globular. the A-B surface of type 2 cytochromes c' is hydrophilic and they take a monomeric or flattened dimeric form. (C) 1998 Academic Press.
  • 菅原 肇, 山本 寛樹, 柴田 直樹, 井上 豪, 三宅 親弘, 横田 明穂, 甲斐 泰
    日本結晶学会誌 40 110-110 1998年  
  • 増田 純, 山口 徹也, 柴田 直樹, 森本 幸生, 飛松 孝正, 虎谷 哲夫, 安岡 則武
    日本結晶学会誌 40 181-181 1998年  
  • 高妻, 孝光, 堀越, 菜穂子, 笹川, 由紀, 井上, 豪, 柴田, 直樹, 甲斐, 泰, 吉崎, 文則, 杉村, 康知, 長友, 重紀, 北川, 禎三
    生物物理 37(2) S168 1997年9月  
  • N Shibata, M Gohow, T Inoue, C Nagano, K Inaba, H Takekuma, SI Takekuma, ZI Yoshida, Y Kai
    ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY 53 335-336 1997年5月  査読有り筆頭著者
    A chromoprotein from Pleurotus salmoneostramineus L. Vass. has been purified and crystallized. The needle-shaped crystal has monoclinic space group C2 with the cell dimensions of a=118.5, b=59.7, c=31.8 Angstrom and B=114 degrees. The crystal diffracts to 1.8 Angstrom resolution with a synchrotron radiation X-ray source.
  • 松本 崇, 柴田 直樹, 森本 幸生, 月原 冨武, 嶋本 伸雄, 安岡 則武
    日本結晶学会誌 39 149-149 1997年  
  • 菅原 肇, 柴田 直樹, 五宝 学, 井上 豪, 甲斐 泰, 武隈 真一, 吉田 善一
    日本結晶学会誌 39 163-163 1997年  
  • 柴田 直樹, 射場 聡明, 岬 真太郎, 樋口 芳樹, 森本 幸生, Meyer T., Cusanovich M.A, 安岡 則武
    日本結晶学会誌 39 150-150 1997年  
  • 須藤 恭子, 柴田 直樹, 森本 幸生, 北村 昌也, 仲谷 忠雄, 安岡 則武
    日本結晶学会誌 39 151-151 1997年  
  • N Shibata, H Yamamoto, T Inoue, K Uemura, A Yokota, Y Kai
    JOURNAL OF BIOCHEMISTRY 120(6) 1064-1066 1996年12月  査読有り筆頭著者
    Ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO) from a red alga, Galdieria partita, has been crystallized by the hanging drop vapor diffusion method, Two forms (Forms I and II) of crystals were obtained under distinct conditions, The Form I crystal belongs to monoclinic space group C2 with cell dimensions of a=190.2, b=140.0, c=189.0 A, and beta=102.6, and diffracts up to 3.0 Angstrom resolution, Diffraction from the Form II crystal was too weak to determine crystal data.
  • N Shibata, T Inoue, K Fukuhara, Y Nagara, R Kitagawa, S Harada, N Kasai, K Uemura, K Kato, A Yokota, Y Kai
    JOURNAL OF BIOLOGICAL CHEMISTRY 271(43) 26449-26452 1996年10月  査読有り筆頭著者
    We determined the crystal structure of spinach ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) by x-ray diffraction at 1.8-Angstrom resolution and found that the enzyme contained two kinds of S, S-I and S-II, present in equal number and disposed in an orderly way within the Rubisco holoenzyme. The electron density maps suggested that leucine was at residue 56 in S-I, although histidine was at that position in S-II. There were other residue differences. Thus, spinach Rubisco has a L(8)S(4)(I)S(II)4 subunit structure. The orderly disposition of the heterogeneous small subunits in the Rubisco holoenzyme provides accounts of a multigene family of S in plants.
  • 柴田 直樹, 五宝 学, 井上 豪, 甲斐 泰, 吉田 善一, 武隈 真一, 武隈 秀子, 松原 義治, 稲葉 和功
    日本結晶学会誌 38 105-105 1996年  
  • 永野 智瑞子, 五宝 学, 柴田 直樹, 井上 豪, 甲斐 泰, 武隈 真一, 武隈 秀子, 吉田 善一
    日本結晶学会誌 37 47-47 1995年  
  • 柴田 直樹, 福原 一浩, 北川 良一, 井上 豪, 甲斐 泰, 横田 明穂
    日本結晶学会誌 37 140-140 1995年  
  • T INOUE, N SHIBATA, H NAKANISHI, S KOYAMA, H ISHII, Y KAI, S HARADA, N KASAI, Y OHSHIRO, S SUZUKI, T KOHZUMA, K YAMAGUCHI, S SHIDARA, H IWASAKI
    JOURNAL OF BIOCHEMISTRY 116(6) 1193-1197 1994年12月  査読有り
    The crystal structure of azurin from a denitrifying bacterium, Achromobacter xylosoxidans NCIE11015, has been refined at 2.5 Angstrom resolution using diffraction data obtained by means of synchrotron radiation at KEK. Crystals suitable for X-ray experiment were obtained by the macro-seeding method and an intensity data were obtained on imaging plates mounted on a Weissenberg camera (R(merge) = 0.09). The initial model was obtained by the molecular replacement method using the structure of azurin from Alcaligenes denitrificans NCTC8582 as a starting model. The structure was refined by molecular dynamics optimization and the restrained least-squares method to a crystallographic R-value of 0.205. However, the current model gave an electron-density of the side-chain regions of several residues close to the N-terminus quite different from those expected from the amino acid sequences reported. Very recently, two kinds of azurins (Az-I and At-II) were isolated from this bacterium by a slightly modified purification method and have been characterized and found to have different CD spectra. On analysis of amino acid sequences around the N-terminus, the second azurin (At-II) was proved to be a new type of azurin in this bacterium. It was consequently revealed that the current model corresponds to a new type of azurin because of the complete agreement between the electron-density and the amino acid sequence of the newly determined 20 residues from the N-terminus. Determination of the whole amino acid sequence of this azurin and further refinement are in progress.
  • 永野 智瑞子, 柴田 直樹, 井上 豪, 甲斐 泰, 鈴木 晋一郎, 山口 和也
    日本結晶学会誌 36 120-120 1994年  
  • 柴田 直樹, 福原 一浩, 井上 豪, 甲斐 泰, 原田 繁春, 横田 明穂
    日本結晶学会誌 36 185-185 1994年  
  • 志波 智生, 松村 浩由, 原田 繁春, 栗栖 源嗣, 柴田 直樹, 井上 豪, 甲斐 泰
    日本結晶学会誌 36 116-116 1994年  

MISC

 65
  • 柴田直樹, 樋口芳樹, 虎谷哲夫
    第468回ビタミンB研究協議会 2022年9月  筆頭著者
  • 根来誠司, 武尾正弘, 柴田直樹, 樋口芳樹, 加藤太一郎, 重田育照
    月刊バイオインダストリー 2019年6月  招待有り
  • Yamanaka Masaru, Hoshizumi Makoto, Nagao Satoshi, Nakayama Ryoko, Shibata Naoki, Higuchi Yoshiki, Hirota Shun
    2017年2月14日  
    The number of artificial protein supramolecules has been increasing; however, control of protein oligomer formation remains challenging. Cytochrome c′ from Allochromatium vinosum (AVCP) is a homodimeric protein in its native form, where its protomer exhibits a four-helix bundle structure containing a covalently bound five-coordinate heme as a gas binding site. AVCP exhibits a unique reversible dimer-monomer transition according to the absence and presence of CO. Herein, domain-swapped dimeric AVCP was constructed and utilized to form a tetramer and high-order oligomers. The X-ray crystal structure of oxidized tetrameric AVCP consisted of two monomer subunits and one domain-swapped dimer subunit, which exchanged the region containing helices αA and αB between protomers. The active site structures of the domain-swapped dimer subunit and monomer subunits in the tetramer were similar to those of the monomer subunits in the native dimer. The subunit-subunit interactions at the interfaces of the domain-swapped dimer and monomer subunits in the tetramer were also similar to the subunit-subunit interaction in the native dimer. Reduced tetrameric AVCP dissociated to a domain-swapped dimer and two monomers upon CO binding. Without monomers, the domain-swapped dimers formed tetramers, hexamers, and higher-order oligomers in the absence of CO, whereas the oligomers dissociated to domain-swapped dimers in the presence of CO, demonstrating that the domain-swapped dimer maintains the CO-induced subunit dissociation behavior of native ACVP. These results suggest that protein oligomer formation may be controlled by utilizing domain swapping for a dimer-monomer transition protein.
  • 衣笠 凌, 羽田 圭吾, 谷本 悠樹, 竹原 一起, 柴田 直樹, 加藤 太一郎, 武尾 正弘, 根来 誠司
    日本生物工学会大会講演要旨集 67 282-282 2015年  
  • Y. Higuchi, M. Akter, C. Inoue, Y. Shomura, N. Shibata, K. Inaka, K. Kataoka, T. Sakurai, K. Komori
    JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY 19 S324-S324 2014年3月  

書籍等出版物

 3

主要な共同研究・競争的資金等の研究課題

 20