Publication | Closed Access
Solution structure of <i>Vibrio cholerae</i> protein VC0424: A variation of the ferredoxin‐like fold
11
Citations
38
References
2003
Year
Solution StructureNmr SpectroscopyBiochemistryStructural BioinformaticsProtein FoldingNatural SciencesVirulence FactorProtein X-ray CrystallographyMolecular BiologyAlpha-beta Sandwich ArchitectureFerredoxin‐like FoldProtein Structure PredictionOrder AlphabetaalphabetabetaalphabetaMicrobiologyMedicineStructural Biology
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.
| Year | Citations | |
|---|---|---|
Page 1
Page 1