1ahe

ASPARTATE AMINOTRANSFERASE HEXAMUTANT

spinqualitylabelsall models 1ahe, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ahe is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: PLP, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function AAT_ECOLI Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aspartate aminotransferase 3D structures

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