1yfe
Crystal structure of apo fumarase C from Escherichia coliCrystal structure of apo fumarase C from Escherichia coli
Structural highlights
FunctionFUMC_ECOLI Catalyzes the reversible addition of water to fumarate to give L-malate.[1] Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedPrevious crystal structures of fumarase C from Escherichia coli have noted two occupied dicarboxylate-binding sites termed the active site and the B site. Here, the first known fumarase C structure is reported in which both sites are unoccupied by bound ligand. This so-called ;free' crystal form shows conservation of the active-site water in a similar orientation to that reported in other fumarase C crystal structures. More importantly, a shift of His129 has been observed at the B site. This new crystallographic information suggests the use of water as a permanent member of the active site and the use of an imidazole-imidazolium conversion to control access at the allosteric B site. Structure of free fumarase C from Escherichia coli.,Weaver T Acta Crystallogr D Biol Crystallogr. 2005 Oct;61(Pt 10):1395-401. Epub, 2005 Sep 28. PMID:16204892[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
|