PMID:12824501

Citation	Ramelot, TA, Ni, S, Goldsmith-Fischman, S, Cort, JR, Honig, B and Kennedy, MA (2003) Solution structure of Vibrio cholerae protein VC0424: a variation of the ferredoxin-like fold. Protein Sci. 12:1556-61
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.
Links	PubMed PMC2323929 Online version:10.1110/ps.03108103
Keywords	Amino Acid Sequence; Ferredoxins/chemistry; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Sequence Data; Protein Conformation; Sequence Alignment; Solutions; Vibrio cholerae/chemistry
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