2DAB

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

2DAB の概要

• エントリーDOI: 10.2210/pdb2dab/pdb
• 分子名称: D-AMINO ACID AMINOTRANSFERASE, PYRIDOXAL-5'-PHOSPHATE (3 entities in total)
• 機能のキーワード: transferase, aminotransferase, pyridoxal-5'-phosphate, d-amino acid, d-alanine, alpha-ketoglutamic acid
• 由来する生物種: Bacillus sp.
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 65033.94

構造登録者

Sugio, S.,Kashima, A.,Kishimoto, K.,Peisach, D.,Petsko, G.A.,Ringe, D.,Yoshimura, T.,Esaki, N. (登録日: 1997-11-30, 公開日: 1998-06-03, 最終更新日: 2023-08-09)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2 Å)