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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structure of the S pilus periplasmic chaperone SfaE at 2.2 A resolution.
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Structure of the S pilus periplasmic chaperone SfaE at 2.2 A resolution.

机译：年代纤毛结构周质的女伴SfaE 2.2一项决议。

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摘要

S pili are sialic acid binding hair-like appendages expressed by pathogenic strains of Escherichia coli. The presence of S pili has been implicated as a virulence factor in both urinary-tract infections and new-born meningitis. Assembly of S pili proceeds via the ubiquitous chaperone/usher pathway. Previously, structures of the homologous chaperones PapD and FimC involved in assembly of P and type-1 pili, respectively, have been solved. Here, the 2.2 A X-ray structure of the S pilus chaperone SfaE is reported. SfaE has the same overall L-shaped structure as PapD and FimC, with two immunoglobulin-like domains oriented at about a 90 degrees angle to each other. Conserved residues in the subunit-binding cleft known to be critical for chaperone function occupy essentially identical positions in SfaE, FimC and PapD. As in free PapD and FimC, the long F1-G1 loop connecting the two last strands of the N-terminal domain is disordered. SfaE crystallizes as a dimer with an extensive dimer interface involving thesubunit-binding surfaces of the chaperone. Dimerization via these regions has previously been observed for PapD and might be a general side effect arising from the subunit-binding properties of periplasmic chaperones. The domain interface contains an extended hydrogen-bond network involving three invariant charged residues and two structurally conserved water molecules. It is suggested that disruption of the domain interactions may destabilize the N-terminal domain through exposure of three conserved hydrophobic residues, thereby promoting release of pilus subunits during pilus assembly.
机译：S pili唾液酸绑定的毛发附件所表达的致病菌株大肠杆菌。涉及的毒力因子尿路感染和新生儿脑膜炎。组装的年代pili通过无处不在的收益伴侣/开启通道。同源的监护人PapD FimC参与组装的P和1型菌毛,分别,已经解决。年代的x射线结构纤毛女伴SfaE报道。PapD和FimC结构——两个面向immunoglobulin-like域有关90度角。残留在subunit-binding间隙伴侣蛋白功能占据的关键本质上相同的职位SfaE, FimC和PapD。循环链的连接两个妻子n端结构域是无序的。结晶是一个二聚体具有广泛的二聚体接口涉及thesubunit-binding表面的女伴。PapD曾被观察到,可能吗一般产生的副作用subunit-binding周质的性能监护人。扩展形成氢键网络涉及三个不变的残留物和两个结构守恒的水分子。混乱的领域可能的交互破坏n端结构域接触三个守恒的疏水残基,从而促进纤毛子单元的释放在毛组装。

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