Ramelot Theresa A, Ni Shuisong, Goldsmith-Fischman Sharon, Cort John R, Honig Barry, Kennedy Michael A
Biological Sciences Division, Pacific Northwest National Laboratory, EMSL 2569 K8-98, 3335 Q Avenue, Richland, WA 99352, USA.
Protein Sci. 2003 Jul;12(7):1556-61. doi: 10.1110/ps.03108103.
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.
霍乱弧菌蛋白VC0424的结构通过核磁共振光谱法测定。VC0424属于一个功能未知的细菌保守蛋白家族(COG 3076)。该结构具有α-β三明治结构,由两层组成:一个四链反平行β折叠片和三个并排的α螺旋。二级结构元件沿序列具有αβαβαβαβ的顺序。这种折叠与铁氧化还原蛋白样折叠相同,只是有一个额外的长N端螺旋,使其成为这种常见基序的一种变体。蛋白质β折叠片一侧的一组保守表面残基形成一个口袋,这可能对这个保守蛋白家族的生物学功能很重要。