1NWC

Crystal Structure of Aspartate-Semialdehyde Dehydrogenase from Haemophilus influenzae

1NWC の概要

• エントリーDOI: 10.2210/pdb1nwc/pdb
• 関連するPDBエントリー: 1BRM 1GL3 1MB4 1MC4
• 分子名称: Aspartate-semialdehyde dehydrogenase (2 entities in total)
• 機能のキーワード: enzyme, aspartate-semialdehyde dehydrogenase, haemophilus influenzae, oxidoreductase
• 由来する生物種: Haemophilus influenzae
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 81167.47

構造登録者

Blanco, J.,Moore, R.A.,Viola, R.E. (登録日: 2003-02-05, 公開日: 2003-11-04, 最終更新日: 2023-08-16)

主引用文献

Blanco, J.,Moore, R.A.,Viola, R.E.
Capture of an Intermediate in the Catalytic Cycle of L-Aspartate-beta-Semialdehyde Dehydrogenase
Proc.Natl.Acad.Sci.USA, 100:12613-12617, 2003

PubMed Abstract: The structural analysis of an enzymatic reaction intermediate affords a unique opportunity to study a catalytic mechanism in extraordinary detail. Here we present the structure of a tetrahedral intermediate in the catalytic cycle of aspartate-beta-semialdehyde dehydrogenase (ASADH) from Haemophilus influenzae at 2.0-A resolution. ASADH is not found in humans, yet its catalytic activity is required for the biosynthesis of essential amino acids in plants and microorganisms. Diaminopimelic acid, also formed by this enzymatic pathway, is an integral component of bacterial cell walls, thus making ASADH an attractive target for the development of new antibiotics. This enzyme is able to capture the substrates aspartate-beta-semialdehyde and phosphate as an active complex that does not complete the catalytic cycle in the absence of NADP. A distinctive binding pocket in which the hemithioacetal oxygen of the bound substrate is stabilized by interaction with a backbone amide group dictates the R stereochemistry of the tetrahedral intermediate. This pocket, reminiscent of the oxyanion hole found in serine proteases, is completed through hydrogen bonding to the bound phosphate substrate.

PubMed: 14559965
DOI: 10.1073/pnas.1634958100

実験手法

X-RAY DIFFRACTION (2.04 Å)