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PROTEIN STRUCTURE REPORT

Solution structure of Vibrio cholerae protein VC0424: A variation of the ferredoxin-like fold

¹ Biological Sciences Division, Pacific Northwest National Laboratory, EMSL 2569 K8-98, Richland, Washington 99352, USA
² Howard Hughes Medical Institute, Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032, USA
³ Northeast Structural Genomics Consortium

Reprint requests to: Michael A. Kennedy, Environmental Molecular Sciences Laboratory 2569 K8-98, Pacific Northwest National Laboratory, 3335 Q Avenue, Richland, WA 99352, USA; e-mail: ma_kennedy{at}pnl.gov; fax: (509) 376-2303.

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 -ß sandwich architecture consisting of two layers: a four-stranded antiparallel ß-sheet and three side-by-side -helices. The secondary structure elements have the order ßßßß 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 ß-sheet side of the protein forms a pocket that may be important for the biological function of this conserved family of proteins.

Keywords: VC0424; COG 3076; YjgD; structural genomics; NMR structure; Vibrio cholerae

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