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6nza

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Crystal structure of E. coli fumarase C K324A variant with closed SS Loop at 1.41 angstrom resolution

Structural highlights

6nza 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 1.406Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FUMC_ECOLI Catalyzes the reversible addition of water to fumarate to give L-malate.^[1]

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Ueda Y, Yumoto N, Tokushige M, Fukui K, Ohya-Nishiguchi H. Purification and characterization of two types of fumarase from Escherichia coli. J Biochem. 1991 May;109(5):728-33. PMID:1917897
↑ Stuttgen GM, Grosskopf JD, Berger CR, May JF, Bhattacharyya B, Weaver TM. Closed fumarase C active-site structures reveal SS Loop residue contribution in catalysis. FEBS Lett. 2020 Jan;594(2):337-357. doi: 10.1002/1873-3468.13603. Epub 2019 Sep, 23. PMID:31514245 doi:http://dx.doi.org/10.1002/1873-3468.13603