1DAA

CRYSTALLOGRAPHIC STRUCTURE OF D-AMINO ACID AMINOTRANSFERASE COMPLEXED WITH PYRIDOXAL-5'-PHOSPHATE

1DAA の概要

• エントリーDOI: 10.2210/pdb1daa/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, d-amino acid, d-alanine, pyridoxal phosphate, transferase (aminotransferase)
• 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: 65118.10

構造登録者

Sugio, S.,Peisach, D.,Ringe, D. (登録日: 1995-06-09, 公開日: 1995-09-15, 最終更新日: 2024-02-07)

主引用文献

Sugio, S.,Petsko, G.A.,Manning, J.M.,Soda, K.,Ringe, D.
Crystal structure of a D-amino acid aminotransferase: how the protein controls stereoselectivity.
Biochemistry, 34:9661-9669, 1995

PubMed Abstract: The three-dimensional structure of D-amino acid aminotransferase (D-AAT) in the pyridoxamine phosphate form has been determined crystallographically. The fold of this pyridoxal phosphate (PLP)-containing enzyme is completely different from those of any of the other enzymes that utilize PLP as part of their mechanism and whose structures are known. However, there are some striking similarities between the active sites of D-AAT and the corresponding enzyme that transaminates L-amino acids, L-aspartate aminotransferase. These similarities represent convergent evolution to a common solution of the problem of enforcing transamination chemistry on the PLP cofactor. Implications of these similarities are discussed in terms of their possible roles in the stabilization of intermediates of a transamination reaction. In addition, sequence similarity between D-AAT and branched chain L-amino acid aminotransferase suggests that this latter enzyme will also have a fold similar to that of D-AAT.

PubMed: 7626635
DOI: 10.1021/bi00030a002

実験手法

X-RAY DIFFRACTION (1.94 Å)