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Structure of the archaeal chemotaxis protein CheY in a domain-swapped dimeric conformation.
Acta Crystallographica Section F ( IF 1.1 ) Pub Date : 2019-08-30 , DOI: 10.1107/s2053230x19010896
Karthik Shivaji Paithankar 1 , Mathias Enderle 1 , David C Wirthensohn 2 , Arthur Miller 2 , Matthias Schlesner 2 , Friedhelm Pfeiffer 3 , Alexander Rittner 1 , Martin Grininger 1 , Dieter Oesterhelt 2
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Archaea are motile by the rotation of the archaellum. The archaellum switches between clockwise and counterclockwise rotation, and movement along a chemical gradient is possible by modulation of the switching frequency. This modulation involves the response regulator CheY and the archaellum adaptor protein CheF. In this study, two new crystal forms and protein structures of CheY are reported. In both crystal forms, CheY is arranged in a domain-swapped conformation. CheF, the protein bridging the chemotaxis signal transduction system and the motility apparatus, was recombinantly expressed, purified and subjected to X-ray data collection.

中文翻译:


结构域交换二聚体构象中古细菌趋化蛋白 CheY 的结构。



古细菌通过古细菌的旋转而运动。古菌在顺时针和逆时针旋转之间切换,并且通过调节切换频率可以沿着化学梯度移动。这种调节涉及反应调节剂 CheY 和古菌衔接蛋白 CheF。在这项研究中,报道了 CheY 的两种新晶体形式和蛋白质结构。在两种晶体形式中,CheY 均以域交换构象排列。 CheF 是连接趋化信号转导系统和运动装置的蛋白质,经过重组表达、纯化并进行 X 射线数据收集。
更新日期:2019-11-01
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