1TB4

Crystal Structure of Aspartate-Semialdehyde Dehydrogenase From Haemophilus influenzae with a Bound Periodate

1TB4 の概要

• エントリーDOI: 10.2210/pdb1tb4/pdb
• 関連するPDBエントリー: 1NWC 1TA4
• 分子名称: Aspartate-semialdehyde dehydrogenase, PERIODATE (3 entities in total)
• 機能のキーワード: aspartate-semialdehyde dehydrogenase, aspartate biosynthetic pathway, periodate, oxidoreductase
• 由来する生物種: Haemophilus influenzae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40774.64

構造登録者

Viola, R.E. (登録日: 2004-05-19, 公開日: 2004-12-07, 最終更新日: 2024-02-14)

主引用文献

Faehnle, C.R.,Blanco, J.,Viola, R.E.
Structural basis for discrimination between oxyanion substrates or inhibitors in aspartate-beta-semialdehyde dehydrogenase.
Acta Crystallogr.,Sect.D, 60:2320-2324, 2004

PubMed Abstract: The reversible dephosphorylation of beta-aspartyl phosphate to L-aspartate-beta-semialdehyde (ASA) in the aspartate biosynthetic pathway is catalyzed by aspartate-beta-semialdehyde dehydrogenase (ASADH). The phosphate that is present to activate the aspartate carboxyl group is held in a separate and distinct binding site once removed and prior to its release from the enzyme. This site had been shown to be selective for tetrahedral oxyanions, with several competitive inhibitors and alternative substrates previously identified for the reverse reaction. Structural studies have now shown that the most potent oxyanion inhibitor (periodate) and a good alternative substrate (arsenate) each occupy the same catalytic phosphate-binding site. However, a rotation of a threonine side chain (Thr137) in the periodate complex disrupts an important hydrogen-bonding interaction with an active-site glutamate (Glu243) that participates in substrate orientation. This subtle change appears to be the difference between a substrate and an inhibitor of this enzyme.

PubMed: 15583380
DOI: 10.1107/S0907444904026411

実験手法

X-RAY DIFFRACTION (2.15 Å)