Solution structure of Vibrio cholerae protein VC0424: a variation of the ferredoxin-like fold |
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Authors: | Ramelot Theresa A Ni Shuisong Goldsmith-Fischman Sharon Cort John R Honig Barry Kennedy Michael A |
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Institution: | Biological Sciences Division, Pacific Northwest National Laboratory, EMSL 2569 K8-98, 3335 Q Avenue, Richland, WA 99352, USA. |
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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. |
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Keywords: | VC0424 COG 3076 YjgD structural genomics NMR structure Vibrio cholerae |
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