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Solution structure of Vibrio cholerae protein VC0424: a variation of the ferredoxin-like fold.

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.

SUBMITTER: Ramelot TA

PROVIDER: S-EPMC2323929 | biostudies-literature | 2003 Jul

REPOSITORIES: biostudies-literature

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Solution structure of Vibrio cholerae protein VC0424: a variation of the ferredoxin-like fold.

Ramelot Theresa A TA Ni Shuisong S Goldsmith-Fischman Sharon S Cort John R JR Honig Barry B Kennedy Michael A MA

Protein science : a publication of the Protein Society 20030701 7

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 a ...[more]

PMID: 12824501

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