6nzc
Crystal structure of E. coli fumarase C N326A variant with closed SS Loop at 1.40 angstrom resolutionCrystal structure of E. coli fumarase C N326A variant with closed SS Loop at 1.40 angstrom resolution
Structural highlights
FunctionFUMC_ECOLI Catalyzes the reversible addition of water to fumarate to give L-malate.[1] Publication Abstract from PubMedFumarase 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. Closed fumarase C active-site structures reveal SS Loop residue contribution in catalysis.,Stuttgen GM, Grosskopf JD, Berger CR, May JF, Bhattacharyya B, Weaver TM FEBS Lett. 2020 Jan;594(2):337-357. doi: 10.1002/1873-3468.13603. Epub 2019 Sep, 23. PMID:31514245[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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