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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Anatomy of secretin binding to the Dickeya dadantii type II secretion system pilotin
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Anatomy of secretin binding to the Dickeya dadantii type II secretion system pilotin

机译:分泌素解剖Dickeya绑定pilotin dadantii II型分泌系统

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The secretins are a family of large multimeric channels in the outer membrane of Gram-negative bacteria that are involved in protein export. In Dickeya dadantii and many other pathogenic bacteria, the lipoprotein pilotin targets the secretin subunits to the outer membrane, allowing a functional type II secretion system to be assembled. Here, the crystal structure of the C-terminal peptide of the secretin subunit bound to its cognate pilotin is reported. In solution, this C-terminal region of the secretin is nonstructured. The secretin peptide folds on binding to the pilotin to form just under four turns of α-helix which bind tightly up against the first helix of the pilotin so that the hydrophobic residues of the secretin helix can bind to the hydrophobic surface of the pilotin. The secretin helix binds parallel to the first part of the fourth helix of the pilotin. An N-capping aspartate encourages helix formation and binding by interacting favourably with the helix dipole of the helical secretin peptide. The structure of the secretin-pilotin complex of the phytopathogenic D. dadantii described here is a paradigm for this interaction in the OutS-PulS family of pilotins, which is essential for the correct assembly of the type II secretion system of several potent human adversaries, including enterohaemorrhagic Escherichia coli and Klebsiella oxytoca.
机译:大型multimeric分泌素是一个家庭渠道的外膜革兰氏阴性细菌参与蛋白质的出口。Dickeya dadantii和许多其他致病细菌,脂蛋白pilotin目标分泌素子单元的外膜,允许一个功能II型分泌系统组装。c端肽的分泌素亚基其同源pilotin报道。这个c端区域分泌素的nonstructured。绑定pilotin形成四个的α螺旋的紧密结合第一个pilotin这样的螺旋疏水残基分泌素的螺旋绑定到pilotin的疏水表面。分泌素螺旋结合平行于第一pilotin第四螺旋的一部分。N-capping天冬氨酸鼓励螺旋的形成通过积极的互动和绑定螺旋螺旋分泌素肽的偶极子。secretin-pilotin复杂的结构这是一个描述植物病原d dadantii范式OutS-PulS这种交互的pilotins家族,这是必不可少的II型分泌系统的正确组装几个强大的人类对手,包括肠出血性大肠杆菌和克雷伯氏菌oxytoca。

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