首页> 外文期刊>Acta crystallographica, Section F. Structural biology and crystallization communications >Crystallization and preliminary X- ray crystallographic analysis of the curli transporter CsgG
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Crystallization and preliminary X- ray crystallographic analysis of the curli transporter CsgG

机译:卷曲运输蛋白CsgG的结晶和初步X射线晶体学分析

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摘要

Gram-negative bacteria have eight known protein secretion systems. The type-VIII secretion system, also known as the curli biosynthesis system, is responsible for the formation of aggregative fibres known in Escherichia coli as curli. Curli are extracellular proteinaceous fibres primarily involved in bacterial biofilm formation and attachment to nonbiotic surfaces. The secretion of curli subunits depends on a dedicated lipoprotein, CsgG, which is found to form an oligomeric secretion channel in the outer membrane. A nonlipidated mutant of CsgG was expressed and crystallized in a soluble form. The crystals diffracted to 3.15 angstrom resolution and belong to space group P1 with a unit cell containing a predicted 16 molecules per asymmetric unit.
机译:革兰氏阴性细菌具有八个已知的蛋白质分泌系统。 VIII型分泌系统,也称为curli生物合成系统,负责形成大肠杆菌中称为curli的聚集纤维。 Curli是细胞外蛋白质纤维,主要参与细菌生物膜的形成以及与非生物表面的附着。 curli亚基的分泌取决于专用的脂蛋白CsgG,发现其在外膜中形成寡聚分泌通道。 CsgG的非脂质突变体被表达并以可溶形式结晶。晶体衍射至3.15埃分辨率,属于空间群P1,其晶胞每个不对称单元包含16个预测分子。

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