1A0G

L201A MUTANT OF D-AMINO ACID AMINOTRANSFERASE COMPLEXED WITH PYRIDOXAMINE-5'-PHOSPHATE

Summary for 1A0G

• Entry DOI: 10.2210/pdb1a0g/pdb
• Descriptor: D-AMINO ACID AMINOTRANSFERASE, 4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE (3 entities in total)
• Functional Keywords: transferase, aminotransferase, pyridoxal-5'-phosphate, d-amino acid, d-alanine, alpha-ketoglutamic acid
• Biological source: Bacillus sp.
• Total number of polymer chains: 2
• Total formula weight: 65036.00

Authors

Sugio, S.,Kashima, A.,Kishimoto, K.,Peisach, D.,Petsko, G.A.,Ringe, D.,Yoshimura, T.,Esaki, N. (deposition date: 1997-11-30, release date: 1998-06-03, Last modification date: 2024-05-22)

Primary citation

Sugio, S.,Kashima, A.,Kishimoto, K.,Peisach, D.,Petsko, G.A.,Ringe, D.,Yoshimura, T.,Esaki, N.
Crystal structures of L201A mutant of D-amino acid aminotransferase at 2.0 A resolution: implication of the structural role of Leu201 in transamination.
Protein Eng., 11:613-619, 1998

PubMed Abstract: 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 site. Detailed comparisons of the structures of the mutant, together with that of the pyridoxamine-5'-phosphate form of the wild-type enzyme, imply that Leu201 would play a crucial role in the transamination reaction by keeping the pyridoxyl ring in the proper location without disturbing its oscillating motion, although the residue seems to not be especially important for the structural integrity of the enzyme.

PubMed: 9749913
DOI: 10.1093/protein/11.8.613

Experimental method

X-RAY DIFFRACTION (2 Å)