6nz9 | pdb_00006nz9

Crystal structure of E. coli fumarase C bound to citrate at 1.53 angstrom resolution

spinqualitylabelsall models 6nz9, resolution 1.53Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6nz9 is a 2 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.528Å Ligands: CIT Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FUMC_ECOLI Catalyzes the reversible addition of water to fumarate to give L-malate. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Fumarase

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