1ahg
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(New page: 200px<br /><applet load="1ahg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ahg, resolution 2.5Å" /> '''ASPARTATE AMINOTRANSF...)
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Revision as of 08:44, 20 November 2007
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ASPARTATE AMINOTRANSFERASE HEXAMUTANT
Overview
Mutation of six residues of Escherichia coli aspartate aminotransferase, results in substantial acquisition of the transamination properties of, tyrosine amino-transferase without loss of aspartate transaminase, activity. X-ray crystallographic analysis of key inhibitor complexes of, the hexamutant reveals the structural basis for this substrate, selectivity. It appears that tyrosine aminotransferase achieves nearly, equal affinities for a wide range of amino acids by an unusual, conformational switch. An active-site arginine residue either shifts its, position to electrostatically interact with charged substrates or moves, aside to allow access of aromatic ligands.
About this Structure
1AHG is a Single protein structure of sequence from Escherichia coli. Active as Aspartate transaminase, with EC number 2.6.1.1 Full crystallographic information is available from OCA.
Reference
Alternating arginine-modulated substrate specificity in an engineered tyrosine aminotransferase., Malashkevich VN, Onuffer JJ, Kirsch JF, Jansonius JN, Nat Struct Biol. 1995 Jul;2(7):548-53. PMID:7664122
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