1ahf: Difference between revisions
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'''ASPARTATE AMINOTRANSFERASE HEXAMUTANT''' | '''ASPARTATE AMINOTRANSFERASE HEXAMUTANT''' | ||
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[[Category: Jansonius, J N.]] | [[Category: Jansonius, J N.]] | ||
[[Category: Malashkevich, V N.]] | [[Category: Malashkevich, V N.]] | ||
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Revision as of 10:16, 2 May 2008
ASPARTATE AMINOTRANSFERASE HEXAMUTANT
OverviewOverview
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 StructureAbout this Structure
1AHF is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
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 Fri May 2 10:16:27 2008