1ahx
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1ahx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ahx, resolution 2.0Å" /> '''ASPARTATE AMINOTRANSF...)
Next diff →
Revision as of 08:45, 20 November 2007
|
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
1AHX is a Single protein structure of sequence from Escherichia coli with PLP and HCI as ligands. 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
Page seeded by OCA on Tue Nov 20 10:52:14 2007
