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J. Biochem, 1997, Vol. 121, No. 4 637-641
© 1997 Japanese Biochemical Society

other

Three-Dimensional Structure of Escherichia coli Branched-Chain Amino Acid Aminotransferase at 2.5 Å Resolution1

Kengo Okada*, Ken Hirotsu*,2, Mamoru Sato{dagger}, Hideyuki Hayashi{ddagger} and Hiroyuki Kagamiyama{ddagger}

*Department of Chemistry, Faculty of Science, Osaka City University Sugimoto, Sumiyoshi-ku, Osaka 558
{dagger}Graduate School of Integrated Science, Yokohama City University Kanazawa-ku, Yokohama 236
{ddagger}Department of Medical Chemistry, Osaka Medical College Takatsuki, Osaka 569

2To whom correspondence should be addressed. Phone: +81-6-605-2557, Fax: +81-6-605-3131, E-mail: hirotsu{at}sci.osaka.cu.ac.jp

The X-ray crystallographic structure of the branched-chain amino acid aminotransferase from Escherichia coli was determined by means of isomorphous replacement using the selenomethionyl enzyme as one of the heavy atom derivatives. The enzyme is a homo hexamer with D3 symmetry, and the polypeptide chain of the subunit is folded into two domains (small and large domains). The coenzyme, pyridoxal 5'-phosphate, resides at the domain interface, its re-face facing toward the protein. The active site structure shows that the following sites can recognize branched-chain amino acids and glutamate as substrates: (1) a hydrophobic core formed by Phe36, Tyr164, Tyr31*, and Val109* for a branched-chain; (2) Arg97 for an acidic side chain of glutamate; and (3) Tyr95 and two main chain NH groups of Thr257 and Ala258 for the {alpha}-carboxylate of substrates. Although the main chain conformation of the active site is homologous to that of D-amino acid aminotransferase, many of the active site residues are different between them.

1This study was supported in part by a Grant-in-Aid for Scientific Research [No. 08214212 (Priority Areas)] from the Ministry of Education, Science, Sports and Culture of Japan, and a research grant from the Japan Society for the Promotion of Science ("Research for the Future Program").


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