1MC4

Crystal Structure of Aspartate-Semialdehyde dehydrogenase from Vibrio Cholerae El Tor

1MC4 の概要

• エントリーDOI: 10.2210/pdb1mc4/pdb
• 関連するPDBエントリー: 1BRM 1GL3 1MB4
• 分子名称: Aspartate-semialdehyde dehydrogenase (2 entities in total)
• 機能のキーワード: enzyme, aspartate-semialdehyde dehydrogenase, vibrio cholerae, oxidoreductase
• 由来する生物種: Vibrio cholerae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40541.66

構造登録者

Blanco, J.,Moore, R.A.,Kabaleeswaran, V.,Viola, R.E. (登録日: 2002-08-05, 公開日: 2003-03-18, 最終更新日: 2024-02-14)

主引用文献

Blanco, J.,Moore, R.A.,Kabaleeswaran, V.,Viola, R.E.
A Structural Basis for the Mechanism of Aspartate-beta-semialdehyde Dehydrogenase from Vibrio Cholerae
Protein Sci., 12:27-33, 2003

PubMed Abstract: L-Aspartate-beta-semialdehyde dehydrogenase (ASADH) catalyzes the reductive dephosphorylation of beta-aspartyl phosphate to L-aspartate-beta-semialdehyde in the aspartate biosynthetic pathway of plants and micro-organisms. The aspartate pathway produces fully one-quarter of the naturally occurring amino acids, but is not found in humans or other eukaryotic organisms, making ASADH an attractive target for the development of new antibacterial, fungicidal, or herbicidal compounds. We have determined the structure of ASADH from Vibrio cholerae in two states; the apoenzyme and a complex with NADP, and a covalently bound active site inhibitor, S-methyl-L-cysteine sulfoxide. Upon binding the inhibitor undergoes an enzyme-catalyzed reductive demethylation leading to a covalently bound cysteine that is observed in the complex structure. The enzyme is a functional homodimer, with extensive intersubunit contacts and a symmetrical 4-amino acid bridge linking the active site residues in adjacent subunits that could serve as a communication channel. The active site is essentially preformed, with minimal differences in active site conformation in the apoenzyme relative to the ternary inhibitor complex. The conformational changes that do occur result primarily from NADP binding, and are localized to the repositioning of two surface loops located on the rim at opposite sides of the NADP cleft.

PubMed: 12493825
DOI: 10.1110/ps.0230803

実験手法

X-RAY DIFFRACTION (2.77 Å)