|Protein Science (2003) 12(7):1556-61|
|Northeast Structural Genomics Consortium|
(click to unfold)
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.
|Models, Molecular Ferredoxins Magnetic Resonance Spectroscopy Molecular Sequence Data Protein Conformation Sequence Alignment Amino Acid Sequence Vibrio cholerae Solutions |
|10 (Last update: 03/18/2017 11:38:12am)|
|Protein Sci. 2003 Jul;12(7):1556-61.|