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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structures of OppA and PstS from Yersinia pestis indicate variability of interactions with transmembrane domains.
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Structures of OppA and PstS from Yersinia pestis indicate variability of interactions with transmembrane domains.

机译：结构的哥哥和pst鼠疫杆菌显示变化的交互跨膜域。

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摘要

Bacterial ATP-binding cassette (ABC) transport systems couple ATP hydrolysis with the uptake and efflux of a wide range of substances across bacterial membranes. These systems are comprised of transmembrane domains, nucleotide binding domains and, in the case of uptake systems, periplasmic binding proteins responsible for binding and presentation of substrate to the transmembrane domains. In pathogenic bacteria, ABC systems are known to play roles in virulence and pathogenicity and the surface localization of some components has made them attractive targets for both vaccine and anti-infective development. Here, the crystallization of five proteins (OppA, PstS, PiuA, YrbD and CysP) from Yersinia pestis, the causative agent of plague, are reported that diffracted to resolution limits ranging from 1.6 to 5 A. The first crystal structures of ABC system components from Y. pestis, OppA and PstS, are also reported here as complexes with their substrates. Comparisons of these two structures with known structures of related proteins suggest that these proteins possess versatility in substrate recognition and variations in protein-protein interactions with their cognate transmembrane domains.
机译：细菌磷酸腺苷磁带(ABC)运输系统ATP水解与吸收流出的各种物质细菌膜。的跨膜域,核苷酸绑定域,在吸收系统的情况下,周质的结合蛋白负责绑定和演示的衬底跨膜域。ABC系统毒性中发挥作用和致病性和表面定位一些组件使得他们有吸引力的目标疫苗和抗感染的发展。在这里,五个蛋白质的结晶(哥哥,pst、PiuA YrbD CysP)从鼠疫杆菌,鼠疫的病原体,报告衍射分辨率限制从1.65。系统组件从鼠疫耶尔森氏菌属,哥哥和pst,也在这里报道复合物与他们吗基板。蛋白质与已知结构的相关建议这些蛋白质具有多功能性底物识别和变化与他们的同源蛋白质-蛋白质之间的关系跨膜域。

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