1ahf

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[[Image:1ahf.gif|left|200px]]
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{{STRUCTURE_1ahf| PDB=1ahf | SCENE= }}
{{STRUCTURE_1ahf| PDB=1ahf | SCENE= }}
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'''ASPARTATE AMINOTRANSFERASE HEXAMUTANT'''
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===ASPARTATE AMINOTRANSFERASE HEXAMUTANT===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 7664122 is the PubMed ID number.
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{{ABSTRACT_PUBMED_7664122}}
==About this Structure==
==About this Structure==
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[[Category: Jansonius, J N.]]
[[Category: Jansonius, J N.]]
[[Category: Malashkevich, V N.]]
[[Category: Malashkevich, V N.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:51:31 2008''

Revision as of 13:51, 30 June 2008

Image:1ahf.png

Template:STRUCTURE 1ahf

ASPARTATE AMINOTRANSFERASE HEXAMUTANT

Template:ABSTRACT PUBMED 7664122

About this Structure

1AHF is a Single protein structure of sequence from Escherichia coli. 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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