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Protein Structural Information Analysis Team





担当: 千田 俊哉 主任研究員


X線結晶構造解析は、生体高分子の立体構造を決定するのに最も広く用いられてきた方法です。
極めて精密な構造を決定できる一方、目的とする生体高分子の結晶を作らなければいけないという困難もあります。

当チームでは、特に生体機能に重要な生体高分子複合体の結晶構造解析に力を入れると共に、蛋白質の精製、結晶化に関しても精力的に技術開発を行っています。

CIA/ASF-Histone-H3-H4複合体
CIA/ASF-Histone-H3-H4複合体
フェレドキシン−フェレドキシン還元酵素複合体
電子伝達複合体
(フェレドキシン−フェレドキシン還元酵素複合体)










2010
Crystallization and preliminary crystallographic analysis of Mn(II)-dependent 2,3-dihydroxybiphenyl 1,2-dioxygenase from Bacillus sp. JF8.
Acta Crystallogr. F66, 282-285.
Senda, M., Hatta, T., Kimbara, K. and Senda, T.

Structure of the histone chaperrone CIA/ASF1-double bromodomain complex linking histone modification and site-specific histone eviction.
Proc. Natl. Acad. Sci. USA. 107, 8153-8158.
Akai, Y., Adachi, N., Hayashi, Y., Eitoku, M., Sano, N., Natsume, R., Kudo, N., Tanokura, M., Senda, T., Horikoshi, M.

Enantioselectivity of haloalkane dehalogenases and its modulation by surface loop engineering.
Angew. Chem. Int. 49, 6111-6115.
Prokop, Z., Sato, Y., Brezovsky, J., Mozga, T., Chaloupkova, R., Koudelakova, T., Jerabek, P., Stepankova, V., Natsume, R., van Leeuwen, J. G. E., Janssen, D. B., Florian, J., Nagata, Y., Senda, T. and Damborsky, J.

Regulatory system of the protocatechuate 4,5-cleavage pathway genes essential for lignin downstream catabolism.
J. Bacteriol. 192, 3394-3405.
Kamimura, N., Takamura, K., Hara, H., Kasai, D., Natsume, R., Senda, T., Katayama, Y., Fukuda, M. and Masai, E.

2009
Theoretical framework for the histone modification network: modifications in the unstructured histone tails form a scale-free network.
Genes Cells. 14, 789-806.
Hayashi, Y., Senda, T., Sano, N. and Horikoshi, M.

Redox control of protein conformation in flavoproteins.
Antioxid. Redox Signal. 11, 1741-1766.
Senda T., Senda, M., Kimura, S. and Ishida T.

Crysatllization and preliminary crystallographic analysis of gallate dioxygenase DesB from Sphingobium sp. SYK-6.
Acta Crystallogr. F65, 1171-1174.
Sugimoto, K., Yamamoto, Y., Antoni S., Senda, M., Kasai, D., Masai, E., Fukuda, M. and Senda, T.

2008
Histone chaperones: thirty years from isolation to elucidation of the mechanisms of nucleosome assembly and disassembly.
Cell. Mol. Life Sci. 65, 414-444.
Eitoku, M., Sato, L., Senda, T. and Horikoshi, M.

Crystal structure of Methanococcus jannaschii TATA box-binding protein.
Genes Cells. 13, 1127-1140.
Adachi, N., Senda, M., Natsume, R., Senda, T. and Horikoshi, M.

Effect of leucine-to-methionine substitutions on the diffraction quality of histone chaperone SET/TAF-Ib/INHAT crystals.
Acta Crystallogr. F64, 960-965.
Senda, M., Muto, S., Horikoshi, M. and Senda, T.

2007
Molecular mechanism of the redox-dependent interaction between NADH-dependent ferredoxin reductase and Rieske-type [2Fe-2S] ferredoxin.
J. Mol. Biol. 373, 382-400.
Senda. M., Kishigami, S., Kimura, S., Fukuda, M., Ishida, T. and Senda, T.

Crystal structure of the radical SAM enzyme catalyzing tricyclic modified base formation in tRNA.
J. Mol. Biol. 372, 1204-1214.
Suzuki, Y., Noma, A., Suzuki, T., Senda, M., Senda. T., Ishitani, R. and Nureki, O.

Structural basis for recognition of cognate tRNA by tyrosyl-tRNA synthetase from these kingdoms.
Nucleic Acid Res. 35, 4289-4300.
Tsunoda, M., Kusakabe, Y., Tanaka, N., Ohno, S., Nakamura, M., Senda, T., Moriguchi, T., Asai, N., Sekine, M., Yokogawa, T., Nishikawa, K. and Nakamura, K. T.

Crystallization and preliminary X-ray analysis of the electron-transfer complex of Rieske-type [2Fe-2S] ferredoxin and NADH-dependent ferredoxin reductase derived from Acidovorax sp. strain KKS102.
Acta Crystallogr. F63, 520-523.
Senda M., Kishigami S., Kimura S. and Senda T.

Crystallization and preliminary X-ray analysis of the reduced Rieske-type [2Fe-2S] ferredoxin derived from Pseudomonas sp. strain KKS102.
Acta Crystallogr. F63, 311-314.
Senda, M., Kishigami, S., Kimura, S. and Senda, T.

Crystallization and preliminary crystallographic analysis of a haloalkane dehalogenase, DbjA, from Bradyrhizobium japonicum USDA110.
Acta Crystallogr. F63, 294-296.
Sato, Y., Natsume, R., Tsuda, M., Damborsky, J., Nagata, Y. and Senda, T.

Relationship between the structure of SET/TAF-Iβ/INHAT and its histone chaperone activity.
Proc. Natl. Acad. Sci. USA. 104, 4285-4290.
Muto, S., Senda, M., Akai, Y., Sato, L., Suzuki, T., Nagai, R., Senda, T. and Horikoshi, M.

Structure and function of the histone chaperone CIA/ASF1 complexed with histones H3 and H4.
Nature. 446, 338-341.
Natsume, R., Eitoku, M., Akai, Y., Sano, N., Horikoshi, M. and Senda, T.

Crystallization and preliminary crystallographic analysis of DtsR1, a carboxyltransferase subunit of acetyl-CoA carboxylase from Corynebacterium glutamicum.
Acta Crystallogr. F63, 120-122.
Yamada, M., Natsume, R., Nakamatsu, T., Horinouchi, S., Kawasaki, H. and Senda, T.

2006
Crystallization and preliminary X-ray analysis of the Rieske-type [2Fe-2S] ferredoxin component of biphenyl dioxygenase from Pseudomonas sp. strain KKS102.
Acta Crystallogr. F62, 590-592.
Senda, M., Kimura, S., Kishigami, S. and Senda, T.

Crystallization and preliminary crystallographic analysis of a catechol 2,3-dioxygenase PheB from Bacillus stearothermophilus BR219.
Acta Crystallogr/ F62, 125-127.
Sugimoto, K., Matsufuzi, K., Ohnuma, H., Senda, M., Fukuda, M. and Senda, T.

2005
Single-turnover kinetics of 2,3-dihydroxybiphenyl 1,2-dioxygenase reacting with 3-formylcatechol.
Biophys Res Commun. 338, 223-229.
Ishida, T., Senda, T., Tanaka, H., Yamamoto, A. and Horiike, K.

Amino acids in positions 48, 52, and 73 differentiate the substrate specificities of the highly homologous chlorocatechol 1,2-dioxygenases CbnA and TcbC.
J Bacteriol. 187, 5427-5436.
Liu, S., Ogawa, N., Senda, T., Hasebe, A. and Miyashita, K.

Tolerance of the Rieske-type [2Fe-2S] cluster in recombinant ferredoxin BphA3 from Pseudomonas sp. KKS102 to histidine ligand mutations.
Biochem J. 388, 869-78.
Kimura S, Kikuchi A, Senda T, Shiro Y, Fukuda M.

2004
Purification, crystallization and preliminary X-ray analysis of Methanococcus jannaschii TATA box-binding protein (TBP).
Acta Crystallogr. D60, 2328-2331.
Adachi N, Natsume R, Senda M, Muto S, Senda T, Horikoshi M.

Crystal structure of the terminal oxygenase component of biphenyl dioxygenase derived from Rhodococcus sp. strain RHA1.
J. Mol. Biol. 342, 1041-1052.
Furusawa, Y., Nagarajan, V., Tanokura, M., Masai, E., Fukuda, M. and Senda, T.

Purification, crystallization and preliminary X-ray diffraction analysis of human oncoprotein SET/TAF-1beta.
Acta Crystallogr. D60, 712-714.
Muto S, Senda M, Adachi N, Suzuki T, Nagai R, Senda T, Horikoshi M.

Crystal structure of a γ-butyrolactone autoregulator receptor protein in Streptomyces coelicolor A3(2).
J. Mol. Biol. 336, 409-419.
Natsume, R., Ohnishi, Y., Senda, T. and Horinouchi, S.

2003
Crystallization of CprB, an autoregulator-receptor protein from Streptomyces coelicolor A3(2).
Acta Crystallogr. D59, 2313-2315.
Natsume, R., Takeshita, R., Sugiyama, M., Ohnishi, Y., Senda, T. and Horinouchi, S.

Crystallization of the terminal oxygenase component of biphenyl dioxygenase derived from Rhodococcus sp. strain RHA1.
Protein and Peptide Letters. 10, 412-417.
Nagarajan, V., Sakurai, N., Kubota, M., Nonaka, T., Nagumo, H., Takeda, H., Nishizaki, T. Masai, E., Fukuda, M. and Senda, T.

Crystal structure of a full-length LysR-type transcriptional regulator, CbnR: unusual combination of two subunit forms and molecular bases for causing and changing DNA bend.
J. Mol. Biol. 328, 555-566.
Muraoka , S., Okumura, R., Ogawa, N., Nonaka, T., Miyashita, K. and Senda, T.

Oxygen affinity of hemoglobin regulates O2 consumption, metabolism, and physical activity.
J. Biol. Chem. 278, 5035-5043.
Shirasawa T, Izumizaki M, Suzuki Y, Ishihara A, Shimizu T, Tamaki M, Huang F, Koizumi K, Iwase M, Sakai H, Tsuchida E, Ueshima K, Inoue H, Koseki H, Senda T, Kuriyama T, Homma I.

Purification and crystallization of a LysR-type transcriptional regulator CbnR from Ralstonia eutropha NH9.
Protein and Peptide Letters, 10, 325-329.
Muraoka, S., Okumura, R., Uragami, Y., Nonaka, T., Ogawa, N., Miyashita, K. and Senda, T.

2002
Crystal structures of the reaction intermediate and its homologue of an extradiol-cleaving catecholic dioxygenase.
J. Mol. Biol. 321, 621-636.
Sato, N., Uragami, Y., Nishizaki, T., Takahashi, Y., Sazaki, G., Sugimoto, K., Nonaka, T., Masai, E., Fukuda, M. and Senda, T.






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