4i4c | pdb_00004i4c

Crystal structure of the protein frsA complexed with unknown ligand

spinqualitylabelsall models 4i4c, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4i4c is a 2 chain structure with sequence from Vibrio vulnificus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 1PG, 6NA, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D9IR22_VIBVL Publication Abstract from PubMed The fermentation-respiration switch (FrsA) protein in Vibrio vulnificus was recently reported to catalyze the cofactor-independent decarboxylation of pyruvate. We now report quantum mechanical/molecular mechenical calculations that examine the energetics of C-C bond cleavage for a pyruvate molecule bound within the putative active site of FrsA. These calculations suggest that the barrier to C-C bond cleavage in the bound substrate is 28 kcal/mol, which is similar to that estimated for the uncatalyzed decarboxylation of pyruvate in water at 25 degrees C. In agreement with the theoretical predictions, no pyruvate decarboxylase activity was detected for recombinant FrsA protein that could be crystallized and structurally characterized. These results suggest that the functional annotation of FrsA as a cofactor-independent pyruvate decarboxylase is incorrect. Computational, structural, and kinetic evidence that Vibrio vulnificus FrsA is not a cofactor-independent pyruvate decarboxylase.,Kellett WF, Brunk E, Desai BJ, Fedorov AA, Almo SC, Gerlt JA, Rothlisberger U, Richards NG Biochemistry. 2013 Mar 19;52(11):1842-4. doi: 10.1021/bi400093y. Epub 2013 Mar 5. PMID:23452154 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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