Solution NMR structure of CD1104B from pathogenic Clostridium difficile reveals a distinct α-helical architecture and provides first structural representative of protein domain family PF14203.
Solution NMR structure of CD1104B from pathogenic Clostridium difficile reveals a distinct α-helical architecture and provides first structural representative of protein domain family PF14203.
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DOI：
10.1007/s10969-013-9164-8
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发表时间：
2013-12
期刊：
影响因子：
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通讯作者：
Szyperski, Thomas
中科院分区：
文献类型：
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作者：
Pulavarti, Surya V S R K;Eletsky, Alexander;Lee, Hsiau-Wei;Acton, Thomas B;Xiao, Rong;Everett, John K;Prestegard, James H;Montelione, Gaetano T;Szyperski, Thomas
难辨梭菌630菌株CD1104B蛋白的68个残基具有明显的全α-螺旋结构。该结构是细菌蛋白结构域家族PF14203（目前有180个成员）功能未知（DUF4319）的第一个代表，并揭示了仅有的两个严格保守残基（Glu 8和Lys 48）的侧链形成盐桥。此外，这两个残基位于最大的表面间隙附近，预计这将有助于参与蛋白质-蛋白质相互作用的表面积。这一点，连同它在转座子CTn4中的编码，表明CD1104B（很可能是Pfam 14230的所有成员）通过与不同细菌物种之间转座子转移所需的其他蛋白质相互作用而起作用。
A high-quality structure of the 68-residue protein CD1104B from Clostridium difficile strain 630 exhibits a distinct all α-helical fold. The structure presented here is the first representative of bacterial protein domain family PF14203 (currently 180 members) of unknown function (DUF4319) and reveals that the side-chains of the only two strictly conserved residues (Glu 8 and Lys 48) form a salt bridge. Moreover, these two residues are located in the vicinity of the largest surface cleft which is predicted to contribute to a surface area involved in protein-protein interactions. This, along with its coding in transposon CTn4, suggests that CD1104B (and very likely all members of Pfam 14230) functions by interacting with other proteins required for the transfer of transposons between different bacterial species.