1a3g: Difference between revisions

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[[Image:1a3g.gif|left|200px]]
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{{STRUCTURE_1a3g|  PDB=1a3g  |  SCENE=  }}  
{{STRUCTURE_1a3g|  PDB=1a3g  |  SCENE=  }}  


'''BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE FROM ESCHERICHIA COLI'''
===BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE FROM ESCHERICHIA COLI===




==Overview==
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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.
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{{ABSTRACT_PUBMED_9163511}}


==About this Structure==
==About this Structure==
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[[Category: Aminotransferase]]
[[Category: Aminotransferase]]
[[Category: Pyridoxal enzyme]]
[[Category: Pyridoxal enzyme]]
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Revision as of 12:55, 30 June 2008

File:1a3g.png

Template:STRUCTURE 1a3g

BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE FROM ESCHERICHIA COLI

Template:ABSTRACT PUBMED 9163511

About this Structure

1A3G is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Three-dimensional structure of Escherichia coli branched-chain amino acid aminotransferase at 2.5 A resolution., Okada K, Hirotsu K, Sato M, Hayashi H, Kagamiyama H, J Biochem. 1997 Apr;121(4):637-41. PMID:9163511

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