1a0g
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L201A MUTANT OF D-AMINO ACID AMINOTRANSFERASE COMPLEXED WITH PYRIDOXAMINE-5'-PHOSPHATE
OverviewOverview
The leucine-to-alanine mutation at residue 201 of D-amino acid, aminotransferase provides a unique enzyme which gradually loses its, activity while catalyzing the normal transamination; the co-enzyme form is, converted from pyridoxal 5'-phosphate to pyridoxamine 5'-phosphate upon, the inactivation [Kishimoto,K., Yoshimura,T., Esaki,N., Sugio,S., Manning,J.M. and Soda,K. (1995) J. Biochem., 117, 691-696]. Crystal, structures of both co-enzyme forms of the mutant enzyme have been, determined at 2.0 A resolution: they are virtually identical, and are, quite similar to that of the wild-type enzyme. Significant differences in, both forms of the mutant are localized only on the bound co-enzyme, the, side chains of Lys145 and Tyr31, and a water molecule sitting on the, putative substrate binding ... [(full description)]
About this StructureAbout this Structure
1A0G is a [Single protein] structure of sequence from [Bacillus sp.] with PMP as [ligand]. Active as [[1]], with EC number [2.6.1.21]. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structures of L201A mutant of D-amino acid aminotransferase at 2.0 A resolution: implication of the structural role of Leu201 in transamination., Sugio S, Kashima A, Kishimoto K, Peisach D, Petsko GA, Ringe D, Yoshimura T, Esaki N, Protein Eng. 1998 Aug;11(8):613-9. PMID:9749913
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