Solution structure of Vibrio cholerae protein VC0424: a variation of the ferredoxin-like fold.
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.
Ramelot
Theresa A
TA
Biological Sciences Division, Pacific Northwest National Laboratory, EMSL 2569 K8-98, 3335 Q Avenue, Richland, WA 99352, USA.
Ni
Shuisong
S
Goldsmith-Fischman
Sharon
S
Cort
John R
JR
Honig
Barry
B
Kennedy
Michael A
MA
D000595:Amino Acid Sequence; D005288:Ferredoxins / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D016415:Sequence Alignment; D012996:Solutions; D014734:Vibrio cholerae / Q000737:chemistry*
D005288:Ferredoxins; D012996:Solutions