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Solution Structure of Vibrio Cholerae Protein VC0424: A Variation of the Ferredoxin-like Fold

Journal Article · · Protein Science
DOI:https://doi.org/10.1110/ps.03108103· OSTI ID:15004148
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) and previously unknown function. The structure has an a-b sandwich architecture consisting of two layers: a four stranded antiparallel b-sheet and three side-by-side a-helices. The secondary structure elements have the order ababbab 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 b-sheet side of the protein forms a pocket that may be important for the biological function of this conserved family of proteins.
Research Organization:
Pacific Northwest National Lab., Richland, WA (US), Environmental Molecular Sciences Lab. (US)
Sponsoring Organization:
US Department of Energy (US)
DOE Contract Number:
AC06-76RL01830
OSTI ID:
15004148
Report Number(s):
PNWD-SA-5995; 2327
Journal Information:
Protein Science, Journal Name: Protein Science Journal Issue: 7 Vol. 12
Country of Publication:
United States
Language:
English

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