Structure, specificity, and mode of interaction for bacterial albumin-binding modules
Structure, specificity, and mode of interaction for bacterial albumin-binding modules
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DOI：
10.1074/jbc.m109943200
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发表时间：
2002-03-08
影响因子：
4.8
通讯作者：
Wikström, M
中科院分区：
文献类型：
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作者：
Johansson, MU;Frick, IM;Wikström, M
我们已经确定了蛋白G，C组和G链球菌的表面蛋白的白蛋白结合结构域的溶液结构。我们发现，它折叠成一个左手的三螺旋束类似的蛋白质PAB从Peptostreenglamnus白蛋白结合结构域。这两个结构域共享59%的序列同一性，是非常热稳定的，并结合到人血清白蛋白上的相同位点。白蛋白结合位点，首先确定的这种结构基序称为GA模块，包括残基跨越第一个环的第三个螺旋的开始，并包括GA模块的最保守的区域。这两个GA模块对来自不同物种的白蛋白具有不同的亲和力，并且它们的白蛋白结合模式分别直接对应于C/G链球菌和大变形杆菌的宿主特异性。这些对GA模块的进化、结构和结合特性的研究强调了细菌适应的能力，并强调了与抗生素使用相关的生态和医学问题。
We have determined the solution structure of an albumin binding domain of protein G, a surface protein of group C and G streptococci. We find that it folds into a left handed three-helix bundle similar to the albumin binding domain of protein PAB from Peptostreptococcus magnus. The two domains share 59% sequence identity, are thermally very stable, and bind to the same site on human serum albumin. The albumin binding site, the first determined for this structural motif known as the GA module, comprises residues spanning the first loop to the beginning of the third helix and includes the most conserved region of GA modules. The two GA modules have different affinities for albumin from different species, and their albumin binding patterns correspond directly to the host specificity of C/G streptococci and P. magnus, respectively. These studies of the evolution, structure, and binding properties of the GA module emphasize the power of bacterial adaptation and underline ecological and medical problems connected with the use of antibiotics.