The structure of Vibrio cholerae protein VC0424 was determined by NMR spectroscopy. VC0424 belongs to a conserved family of bacterial proteins of unknown function (COG 3076) and previously unknown function. The structure has an a-b sandwich architecture consisting of two layers: a four stranded antiparallel b-sheet and three side-by-side a-helices. The secondary structure elements have the order ababbab along the sequence. This fold is the same as the ferredoxin-like fold, except with an additional long N-terminal helix, making it a variation on this common motif. A cluster of conserved surface residues on the b-sheet side of the protein forms a pocket that may be important for the biological function of this conserved family of proteins.
Revised: June 29, 2004 |
Published: June 23, 2003
Citation
Ramelot T.A., S. Ni, S. Goldsmith-Fischman, J.R. Cort, B. Honig, and M.A. Kennedy. 2003.Solution Structure of Vibrio Cholerae Protein VC0424: A Variation of the Ferredoxin-like Fold.Protein Science 12, no. 7:1556-1561. PNWD-SA-5995.