6NZB

Crystal structure of E. coli fumarase C S318A variant with closed SS Loop at 1.37 angstrom resolution

6NZB の概要

• エントリーDOI: 10.2210/pdb6nzb/pdb
• 分子名称: Fumarate hydratase class II, CITRIC ACID (3 entities in total)
• 機能のキーワード: fumarase, metabolism, krebs cycle, citrate, lyase
• 由来する生物種: Escherichia coli (strain K12)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 103215.48

構造登録者

Weaver, T.M.,May, J.F.,Bhattacharyya, B. (登録日: 2019-02-13, 公開日: 2019-09-25, 最終更新日: 2023-10-11)

主引用文献

Stuttgen, G.M.,Grosskopf, J.D.,Berger, C.R.,May, J.F.,Bhattacharyya, B.,Weaver, T.M.
Closed fumarase C active-site structures reveal SS Loop residue contribution in catalysis.
Febs Lett., 594:337-357, 2020

PubMed Abstract: Fumarase C (FumC) catalyzes the reversible conversion of fumarate to S-malate. Previous structural investigations within the superfamily have reported a dynamic structural segment, termed the SS Loop. To date, active-site asymmetry has raised the question of how SS Loop placement affects participation of key residues during the reaction. Herein, we report structural and kinetic analyses from Escherichia coli FumC variants to understand the contribution of SS Loop residues S318, K324, and N326. High-resolution X-ray crystallographic results reveal three distinct FumC active-site conformations; disordered-open, ordered-open, and the newly discovered ordered-closed. Surprisingly, each SS Loop variant has unaffected Michaelis constants coupled to reductions in turnover number. Based upon our structural and functional analyses, we propose structural and catalytic roles for each of the aforementioned residues.

PubMed: 31514245
DOI: 10.1002/1873-3468.13603

実験手法

X-RAY DIFFRACTION (1.37 Å)