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Solution structure of Vibrio cholerae protein VC0424: a variation of the ferredoxin-like fold
Authors:Ramelot Theresa A  Ni Shuisong  Goldsmith-Fischman Sharon  Cort John R  Honig Barry  Kennedy Michael A
Institution:Biological Sciences Division, Pacific Northwest National Laboratory, EMSL 2569 K8-98, 3335 Q Avenue, Richland, WA 99352, USA.
Abstract: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). The structure has an alpha-beta sandwich architecture consisting of two layers: a four-stranded antiparallel beta-sheet and three side-by-side alpha-helices. The secondary structure elements have the order alphabetaalphabetabetaalphabeta 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 beta-sheet side of the protein forms a pocket that may be important for the biological function of this conserved family of proteins.
Keywords:VC0424  COG 3076  YjgD  structural genomics  NMR structure  Vibrio cholerae
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