首页> 美国卫生研究院文献>Acta Crystallographica Section F: Structural Biology and Crystallization Communications >Preliminary X-ray diffraction analysis of YcdB from Escherichia coli: a novel haem-containing and Tat-­secreted periplasmic protein with a potential role in iron transport
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Preliminary X-ray diffraction analysis of YcdB from Escherichia coli: a novel haem-containing and Tat-­secreted periplasmic protein with a potential role in iron transport

机译:大肠杆菌YcdB的初步X射线衍射分析:一种新型的含血红素和Tat分泌的周质蛋白在铁运输中具有潜在作用

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摘要

YcdB is a periplasmic haem-containing protein from Escherichia coli that has a potential role in iron transport. It is currently the only reported haem-containing Tat-secreted substrate. Here, the overexpression, purification, crystallization and structure determination at 2.0 Å resolution are reported for the apo form of the protein. The apo-YcdB structure resembles those of members of the haem-dependent peroxidase family and thus confirms that YcdB is also a member of this family. Haem-soaking experiments with preformed apo-YcdB crystals have been optimized to successfully generate haem-containing YcdB crystals that diffract to 2.9 Å. Completion of model building and structure refinement are under way.
机译:YcdB是一种来自大肠埃希菌的周质血红蛋白,在铁运输中具有潜在作用。它是目前唯一报道的含血红素分泌的Tat的底物。在这里,报告了载脂蛋白形式的过表达,纯化,结晶和在2.0Å分辨率下的结构测定。 apo-YcdB结构类似于血红素依赖性过氧化物酶家族的成员,因此证实YcdB也是该家族的成员。已对预先形成的apo-YcdB晶体进行的浸血实验进行了优化,以成功生成衍射到2.9?Å的含血红素的YcdB晶体。模型的建立和结构的完善正在进行中。

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