1ahf: Difference between revisions

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{{Seed}}
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{{STRUCTURE_1ahf|  PDB=1ahf  |  SCENE=  }}  
{{STRUCTURE_1ahf|  PDB=1ahf  |  SCENE=  }}  


'''ASPARTATE AMINOTRANSFERASE HEXAMUTANT'''
===ASPARTATE AMINOTRANSFERASE HEXAMUTANT===




==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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{{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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