Download MendeleySolution structure of Vibrio cholerae protein VC0424: a variation of the ferredoxin-like fold.
Ramelot, T.A., Ni, S., Goldsmith-Fischman, S., Cort, J.R., Honig, B., Kennedy, M.A.(2003) Protein Sci 12: 1556-1561
- PubMed: 12824501
- DOI: https://doi.org/10.1110/ps.03108103
- Primary Citation of Related Structures:
1NXI - PubMed 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.
Organizational Affiliation:
Biological Sciences Division, Pacific Northwest National Laboratory, EMSL 2569 K8-98, 3335 Q Avenue, Richland, WA 99352, USA.
