메뉴 건너뛰기




Volumn 121, Issue 4, 1997, Pages 637-641

Three-dimensional structure of Escherichia coli branched-chain amino acid aminotransferase at 2.5 Å resolution

Author keywords

Branched chain amino acid aminotransferase; Pyridoxal enzyme; Substrate recognition; Three dimensional structure; X ray crystallography

Indexed keywords

AMINOTRANSFERASE; BACTERIAL ENZYME; BRANCHED CHAIN AMINO ACID; GLUTAMIC ACID; PYRIDOXAL 5 PHOSPHATE;

EID: 0030979116     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021633     Document Type: Article
Times cited : (60)

References (25)
  • 2
    • 0026751404 scopus 로고
    • X-ray structure refinement and comparison of three forms of mitochondrial aspartate aminotransferase
    • Mcphalen, C.A., Vincent, M.G., and Jansonius, J.N. (1992) X-ray structure refinement and comparison of three forms of mitochondrial aspartate aminotransferase. J. Mol. Biol. 225, 495-517
    • (1992) J. Mol. Biol. , vol.225 , pp. 495-517
    • Mcphalen, C.A.1    Vincent, M.G.2    Jansonius, J.N.3
  • 3
    • 0027738034 scopus 로고
    • Crystal structures of true enzymatic reaction intermediates: Aspartate and glutamate ketimines in aspartate aminotransferase
    • Malashkevich, V.N., Toney, M.D., and Jansonius, J.N. (1993) Crystal structures of true enzymatic reaction intermediates: aspartate and glutamate ketimines in aspartate aminotransferase. Biochemistry 32, 13451-13462
    • (1993) Biochemistry , vol.32 , pp. 13451-13462
    • Malashkevich, V.N.1    Toney, M.D.2    Jansonius, J.N.3
  • 5
    • 0028174289 scopus 로고
    • Crystal structures of Escherichia coli aspartate aminotransferase in two conformations. Comparison of an unliganded open and two liganded closed forms
    • Jäger, J., Moser, M., Sauder, U., and Jansonius, J.N. (1994) Crystal structures of Escherichia coli aspartate aminotransferase in two conformations. Comparison of an unliganded open and two liganded closed forms. J. Mol. Biol. 239, 285-305
    • (1994) J. Mol. Biol. , vol.239 , pp. 285-305
    • Jäger, J.1    Moser, M.2    Sauder, U.3    Jansonius, J.N.4
  • 6
    • 0028167665 scopus 로고
    • X-Ray crystallographic study of pyridoxal 5′-phosphate-type aspartate aminotransferase from Escherichia coli in open and closed form
    • Okamoto, A., Higuchi, T., Hirotsu, K., Kuramitsu, S., and Kagamiyama, H. (1994) X-Ray crystallographic study of pyridoxal 5′-phosphate-type aspartate aminotransferase from Escherichia coli in open and closed form. J. Biochem. 116, 95-107
    • (1994) J. Biochem. , vol.116 , pp. 95-107
    • Okamoto, A.1    Higuchi, T.2    Hirotsu, K.3    Kuramitsu, S.4    Kagamiyama, H.5
  • 7
    • 0028028030 scopus 로고
    • X-Ray crystallographic study of pyridoxamine 5′-phosphate-type aspartate aminotransferase from Escherichia coli in three forms
    • Miyahara, I., Hirotsu, K., Hayashi, H., and Kagamiyama, H. (1994) X-Ray crystallographic study of pyridoxamine 5′-phosphate-type aspartate aminotransferase from Escherichia coli in three forms. J. Biochem. 116, 1001-1012
    • (1994) J. Biochem. , vol.116 , pp. 1001-1012
    • Miyahara, I.1    Hirotsu, K.2    Hayashi, H.3    Kagamiyama, H.4
  • 8
    • 0029144437 scopus 로고
    • Crystal structure of a D-amino acid aminotransferase: How the protein controls stereoselectivity
    • Sugio, S., Petsko, G.A., Manning, J.M., Soda, K., and Ringe, D. (1995) Crystal structure of a D-amino acid aminotransferase: How the protein controls stereoselectivity. Biochemistry 34, 9661-9669
    • (1995) Biochemistry , vol.34 , pp. 9661-9669
    • Sugio, S.1    Petsko, G.A.2    Manning, J.M.3    Soda, K.4    Ringe, D.5
  • 9
    • 0021909278 scopus 로고
    • Branched-chain amino acid aminotransferase of Escherichia coli: Nucleotide sequence of the ilvE gene and the deduced amino acid sequence
    • Kuramitsu, S., Ogawa, T., Ogawa, H., and Kagamiyama, H. (1985) Branched-chain amino acid aminotransferase of Escherichia coli: nucleotide sequence of the ilvE gene and the deduced amino acid sequence. J. Biochem. 97, 993-999
    • (1985) J. Biochem. , vol.97 , pp. 993-999
    • Kuramitsu, S.1    Ogawa, T.2    Ogawa, H.3    Kagamiyama, H.4
  • 11
    • 12044253901 scopus 로고
    • Unique stereospecificity of D-amino acid aminotransferase and branched-chain L-amino acid aminotransferase for C-4 hydrogen transfer of the coenzyme
    • Yoshimura, T., Nishimura, K., Ito, J., Esaki, N., Kagamiyama, H., Manning, J.M., and Soda, K. (1993) Unique stereospecificity of D-amino acid aminotransferase and branched-chain L-amino acid aminotransferase for C-4 hydrogen transfer of the coenzyme. J. Am. Chem. Soc. 115, 3897-3900
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 3897-3900
    • Yoshimura, T.1    Nishimura, K.2    Ito, J.3    Esaki, N.4    Kagamiyama, H.5    Manning, J.M.6    Soda, K.7
  • 12
    • 0024347444 scopus 로고
    • Crystallization and preliminary X-ray characterization of branched-chain amino acid aminotransferase from Escherichia coli
    • Kamitori, S., Odagaki, Y., Inoue, K., Kuramitsu, S., Kagamiyama, H., Matsuura, Y., and Higuchi, T. (1989) Crystallization and preliminary X-ray characterization of branched-chain amino acid aminotransferase from Escherichia coli. J. Biochem. 105, 671-672
    • (1989) J. Biochem. , vol.105 , pp. 671-672
    • Kamitori, S.1    Odagaki, Y.2    Inoue, K.3    Kuramitsu, S.4    Kagamiyama, H.5    Matsuura, Y.6    Higuchi, T.7
  • 13
    • 0001455061 scopus 로고
    • Weissenberg camera for macromolocules with imaging plate data collection system at the Photon Factory: Present status and future plan (invited)
    • Sakabe, N., Ikemizu, S., Sakabe, K., Higashi, T., Nakagawa, A., Watanabe, N., Adachi, S., and Sasaki, K. (1995) Weissenberg camera for macromolocules with imaging plate data collection system at the Photon Factory: Present status and future plan (invited). Rev. Sci. Instrum. 66, 1276-1281
    • (1995) Rev. Sci. Instrum. , vol.66 , pp. 1276-1281
    • Sakabe, N.1    Ikemizu, S.2    Sakabe, K.3    Higashi, T.4    Nakagawa, A.5    Watanabe, N.6    Adachi, S.7    Sasaki, K.8
  • 14
    • 0028103275 scopus 로고
    • The CCP4 suite: Program for protein crystallography
    • Collaborative Computational Project, Number 4. (1994) The CCP4 suite: program for protein crystallography. Acta Crystallogr. D50, 760-763
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 15
    • 0025262173 scopus 로고
    • Selenomethionyl proteins produced for analysis by multiwave-length anomalous diffraction (MAD): A vehicle for direct determination of three-dimensional structure
    • Hendrickson, W.A., Horton, J.R., and LeMaster, D.M. (1990) Selenomethionyl proteins produced for analysis by multiwave-length anomalous diffraction (MAD): a vehicle for direct determination of three-dimensional structure. EMBO J. 9, 1665-1672
    • (1990) EMBO J. , vol.9 , pp. 1665-1672
    • Hendrickson, W.A.1    Horton, J.R.2    Lemaster, D.M.3
  • 16
    • 0002452464 scopus 로고
    • Data collection and processing
    • SERC Daresbury Laboratory, Warrington
    • Otwinowski, Z. (1993) Data collection and processing in Proceedings of the CCP4 Study Weekend, pp. 56-62, SERC Daresbury Laboratory, Warrington
    • (1993) Proceedings of the CCP4 Study Weekend , pp. 56-62
    • Otwinowski, Z.1
  • 17
    • 0022325950 scopus 로고
    • Resolution of phase ambiguity in macromolecular crystallography
    • Wang, B.-C. (1985) Resolution of phase ambiguity in macromolecular crystallography. Methods Enzymol. 115, 90-112
    • (1985) Methods Enzymol. , vol.115 , pp. 90-112
    • Wang, B.-C.1
  • 18
    • 14444280477 scopus 로고
    • Geometric sources of redundancy in intensity data and their use for phase determination
    • Bricogne, G. (1974) Geometric sources of redundancy in intensity data and their use for phase determination. Acta Crystallogr. A42, 140-149
    • (1974) Acta Crystallogr. , vol.A42 , pp. 140-149
    • Bricogne, G.1
  • 19
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.-Y., Cowan, S.W., and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A47, 110-119
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 20
    • 0023140814 scopus 로고
    • Crystallographic R factor refinement by molecular dynamics
    • Brünger, A.T., Kuriyan, J., and Karplus, M. (1987) Crystallographic R factor refinement by molecular dynamics. Science 235, 458-460
    • (1987) Science , vol.235 , pp. 458-460
    • Brünger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 21
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S., and Thornton, J.M. (1993) PROCHECK: A program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 22
    • 0026664513 scopus 로고
    • Role of Asp222 in the catalytic mechanism of Escherichia coli aspartate aminotransferase: The amino acid residue which enhances the function of the enzyme-bound coenzyme pyridoxal 5′-phosphate
    • Yano, T., Kuramitsu, S., Tanase, S., Morino, Y., and Kagamiyama, H. (1992) Role of Asp222 in the catalytic mechanism of Escherichia coli aspartate aminotransferase: The amino acid residue which enhances the function of the enzyme-bound coenzyme pyridoxal 5′-phosphate. Biochemistry 31, 5878-5887
    • (1992) Biochemistry , vol.31 , pp. 5878-5887
    • Yano, T.1    Kuramitsu, S.2    Tanase, S.3    Morino, Y.4    Kagamiyama, H.5
  • 23
    • 0027757040 scopus 로고
    • Role of an active site residue analyzed by combination of mutagenesis and coenzyme analogue
    • Yano, T., Hinoue, Y., Chen, V.J., Metzler, D.E., Miyahara, I., Hirotsu, K., and Kagamiyama, H. (1993) Role of an active site residue analyzed by combination of mutagenesis and coenzyme analogue. J. Mol. Biol. 234, 1218-1229
    • (1993) J. Mol. Biol. , vol.234 , pp. 1218-1229
    • Yano, T.1    Hinoue, Y.2    Chen, V.J.3    Metzler, D.E.4    Miyahara, I.5    Hirotsu, K.6    Kagamiyama, H.7
  • 24
    • 0025819033 scopus 로고
    • Tyr225 in aspartate aminotransferase: Contribution of the hydrogen bond between Tyr225 and coenzyme to the catalytic reaction
    • Inoue, K., Kuramitsu, S., Okamoto, A., Hirotsu, K., Higuchi, T., Morino, Y., and Kagamiyama, H. (1991) Tyr225 in aspartate aminotransferase: contribution of the hydrogen bond between Tyr225 and coenzyme to the catalytic reaction. J. Biochem. 109, 570-576
    • (1991) J. Biochem. , vol.109 , pp. 570-576
    • Inoue, K.1    Kuramitsu, S.2    Okamoto, A.3    Hirotsu, K.4    Higuchi, T.5    Morino, Y.6    Kagamiyama, H.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.