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首页> 外文期刊>Acta crystallographica. Section F, Structural biology communications >Expression, purification, crystallization and X-ray crystallographic analysis of the periplasmic binding protein VatD from Vibrio vulnificus M2799
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Expression, purification, crystallization and X-ray crystallographic analysis of the periplasmic binding protein VatD from Vibrio vulnificus M2799

机译:来自VibrioVibriofificus M2799的周质结合蛋白常数的表达,纯化,结晶和X射线晶体分析

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摘要

Vibrio vulnificus is a halophilic marine microorganism which causes gastroenteritis and primary septicaemia in humans. An important factor that determines the survival of V. vulnificus in the human body is its ability to acquire iron. VatD is a periplasmic siderophore-binding protein from V. vulnificus M2799. The current study reports the expression, purification and crystallization of VatD. Crystals of both apo VatD and a VatD-desferrioxamine B-Fe3+ (VatD-FOB) complex were obtained. The crystal of apo VatD belonged to space group P6(4)22, while the crystal of the VatD-FOB complex belonged to space group P2(1). The difference in the two crystal forms could be caused by the binding of FOB to VatD.
机译:Vibrio Wulnificus是一种嗜盐海洋微生物,导致人类的胃肠炎和原发性败血症。 确定人体V.Vulnificus的存活的一个重要因素是获得铁的能力。 VATD是来自V.Vulnificus M2799的周质阳光结合蛋白。 目前的研究报告了VATD的表达,纯化和结晶。 得到APO VATD和VATD-脱硫胺B-FE3 +(VATD-FOB)复合物的晶体。 APO VATD的晶体属于空间组P6(4)22,而VATD-FOB复合物的晶体属于空间组P2(1)。 两种晶体形式的差异可能是由FOB与VATD的结合引起的。

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