| Literature DB >> 12824501 |
Theresa A Ramelot1, Shuisong Ni, Sharon Goldsmith-Fischman, John R Cort, Barry Honig, Michael A Kennedy.
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.Entities:
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Year: 2003 PMID: 12824501 PMCID: PMC2323929 DOI: 10.1110/ps.03108103
Source DB: PubMed Journal: Protein Sci ISSN: 0961-8368 Impact factor: 6.725