5JIS

The Crystal Structure of O-acetyl serine sulfhydralase from Brucella abortus

5JIS の概要

• エントリーDOI: 10.2210/pdb5jis/pdb
• 関連するPDBエントリー: 5JJC
• 分子名称: Cysteine synthase (2 entities in total)
• 機能のキーワード: transferase
• 由来する生物種: Brucella abortus S19
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 152154.97

構造登録者

Dharavath, S.,Gourinath, S. (登録日: 2016-04-22, 公開日: 2017-04-05, 最終更新日: 2023-11-15)

主引用文献

Dharavath, S.,Raj, I.,Gourinath, S.
Structure-based mutational studies of O-acetylserine sulfhydrylase reveal the reason for the loss of cysteine synthase complex formation in Brucella abortus
Biochem. J., 474:1221-1239, 2017

PubMed Abstract: Cysteine biosynthesis takes place via a two-step pathway in bacteria, fungi, plants and protozoan parasites, but not in humans, and hence, the machinery of cysteine biosynthesis is an opportune target for therapeutics. The decameric cysteine synthase complex (CSC) is formed when the C-terminal tail of serine acetyltransferase (SAT) binds in the active site of -acetylserine sulfydrylase (OASS), playing a role in the regulation of this pathway. Here, we show that OASS from (BaOASS) does not interact with its cognate SAT C-terminal tail. Crystal structures of native BaOASS showed that residues Gln96 and Tyr125 occupy the active-site pocket and interfere with the entry of the SAT C-terminal tail. The BaOASS (Q96A-Y125A) mutant showed relatively strong binding ( = 32.4 μM) to BaSAT C-terminal peptides in comparison with native BaOASS. The mutant structure looks similar except that the active-site pocket has enough space to bind the SAT C-terminal end. Surface plasmon resonance results showed a relatively strong (7.3 μM ) interaction between BaSAT and the BaOASS (Q96A-Y125A), but no interaction with native BaOASS. Taken together, our observations suggest that the CSC does not form in .

PubMed: 28126739
DOI: 10.1042/BCJ20161062

実験手法

X-RAY DIFFRACTION (2.2 Å)