1FCJ

CRYSTAL STRUCTURE OF OASS COMPLEXED WITH CHLORIDE AND SULFATE

1FCJ の概要

• エントリーDOI: 10.2210/pdb1fcj/pdb
• 関連するPDBエントリー: 1D6S 1OAS
• 分子名称: O-ACETYLSERINE SULFHYDRYLASE, SULFATE ION, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: homodimer, lyase
• 由来する生物種: Salmonella typhimurium
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 139396.32

構造登録者

Burkhard, P.,Tai, C.,Jansonius, J.N.,Cook, P.F. (登録日: 2000-07-18, 公開日: 2000-10-18, 最終更新日: 2025-03-26)

主引用文献

Burkhard, P.,Tai, C.H.,Jansonius, J.N.,Cook, P.F.
Identification of an allosteric anion-binding site on O-acetylserine sulfhydrylase: structure of the enzyme with chloride bound.
J.Mol.Biol., 303:279-286, 2000

PubMed Abstract: A new crystal structure of O-acetylserine sulfhydrylase (OASS) has been solved with chloride bound at an allosteric site and sulfate bound at the active site. The bound anions result in a new "inhibited" conformation, that differs from the "open" native or "closed" external aldimine conformations. The allosteric site is located at the OASS dimer interface. The new inhibited structure involves a change in the position of the "moveable domain" (residues 87-131) to a location that differs from that in the open or closed forms. Formation of the external aldimine with substrate is stabilized by interaction of the alpha-carboxyl group of the substrate with a substrate-binding loop that is part of the moveable domain. The inhibited conformation prevents the substrate-binding loop from interacting with the alpha-carboxyl group, and hinders formation of the external Schiff base and thus subsequent chemistry. Chloride may be an analog of sulfide, the physiological inhibitor. Finally, these results suggest that OASS represents a new class of PLP-dependent enzymes that is regulated by small anions.

PubMed: 11023792
DOI: 10.1006/jmbi.2000.4109

実験手法

X-RAY DIFFRACTION (2 Å)