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首页> 外文期刊>Journal of structural and functional genomics >Crystal structure of the YajQ protein from Haemophilus influenzae reveals a tandem of RNP-like domains
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Crystal structure of the YajQ protein from Haemophilus influenzae reveals a tandem of RNP-like domains

机译：来自流感嗜血杆菌的YajQ蛋白的晶体结构揭示了串联的RNP样结构域

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摘要

A hypothetical protein encoded by the gene YajQ of Haemophilus influenzae was selected, as part of a structural genomics project, for X-ray crystallographic structure determination and analysis to assist with the functional assignment. The protein is present in most bacteria, but not in archaea or eukaryotes. The amino acid sequence has no homology to that of other proteins.The YajQ protein was cloned, expressed, and the crystal structure determined at 2.1-? resolution by applying the multiwavelength anomalous dispersion method to a mercury derivative. The polypeptide chain is folded into two domains with identical folding topology. Each domain has a four-stranded antiparallel β-sheet flanked on one side by two α-helices. This structural motif is a characteristic feature of many RNA-binding proteins. The tetrameric structure observed in the crystal suggests a possibility of binding two stretches of double-stranded nucleic acid.
机译：作为结构基因组计划的一部分，选择了由流感嗜血杆菌基因YajQ编码的假想蛋白质，用于X射线晶体学结构测定和分析，以协助进行功能分配。该蛋白质存在于大多数细菌中，但不存在于古细菌或真核生物中。该氨基酸序列与其他蛋白质没有同源性。YajQ蛋白质被克隆，表达并在2.1-β处确定晶体结构。通过将多波长异常色散方法应用于汞衍生物可实现高分辨率。多肽链被折叠成具有相同折叠拓扑的两个域。每个结构域具有一个四链的反平行β-折叠，其两侧是两个α-螺旋。这种结构基序是许多RNA结合蛋白的特征。在晶体中观察到的四聚体结构表明可能结合两条伸展的双链核酸。

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