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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Jun 1;68(Pt 6):713-5. doi: 10.1107/S174430911201826X. Epub 2012 May 24.
2
Crystallization and preliminary X-ray crystallographic analysis of CheW from Thermotoga maritima: a coupling protein of CheA and the chemotaxis receptor.嗜热栖热菌CheW的结晶及初步X射线晶体学分析：CheA与趋化性受体的偶联蛋白
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3
Structure of the ternary complex formed by a chemotaxis receptor signaling domain, the CheA histidine kinase, and the coupling protein CheW as determined by pulsed dipolar ESR spectroscopy.通过脉冲偶极电子自旋共振波谱法测定由趋化受体信号结构域、CheA 组氨酸激酶和偶联蛋白 CheW 形成的三元复合物的结构。
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4
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The 3.2 Å resolution structure of a receptor: CheA:CheW signaling complex defines overlapping binding sites and key residue interactions within bacterial chemosensory arrays.3.2Å 分辨率的受体：CheA:CheW 信号复合物结构定义了细菌化学感应域内重叠的结合位点和关键残基相互作用。
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6
Crystallization and preliminary X-ray analysis of Thermotoga maritima ribosome recycling factor.嗜热栖热菌核糖体循环因子的结晶及初步X射线分析
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7
Crystallization and preliminary X-ray crystallographic analysis of Escherichia coli CheA P3 dimerization domain.大肠杆菌CheA P3二聚化结构域的结晶及初步X射线晶体学分析
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X-ray crystallographic studies of HemK from Thermotoga maritima, an N5-glutamine methyltransferase.来自嗜热栖热菌的N5-谷氨酰胺甲基转移酶HemK的X射线晶体学研究。
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本文引用的文献

1
Processing of X-ray diffraction data collected in oscillation mode.振荡模式下收集的X射线衍射数据的处理。
Methods Enzymol. 1997;276:307-26. doi: 10.1016/S0076-6879(97)76066-X.
2
Structure of the ternary complex formed by a chemotaxis receptor signaling domain, the CheA histidine kinase, and the coupling protein CheW as determined by pulsed dipolar ESR spectroscopy.通过脉冲偶极电子自旋共振波谱法测定由趋化受体信号结构域、CheA 组氨酸激酶和偶联蛋白 CheW 形成的三元复合物的结构。
Biochemistry. 2010 May 11;49(18):3824-41. doi: 10.1021/bi100055m.
3
CheA Kinase of bacterial chemotaxis: chemical mapping of four essential docking sites.细菌趋化作用的CheA激酶：四个必需对接位点的化学图谱
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Reconstruction of the chemotaxis receptor-kinase assembly.趋化性受体-激酶组装体的重建。
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Collaborative signaling by bacterial chemoreceptors.细菌化学感受器的协同信号传导。
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Making sense of it all: bacterial chemotaxis.理解这一切：细菌趋化性。
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Receptor clustering and signal processing in E. coli chemotaxis.大肠杆菌趋化作用中的受体聚集与信号处理
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8
Subunit exchange by CheA histidine kinases from the mesophile Escherichia coli and the thermophile Thermotoga maritima.来自嗜温菌大肠杆菌和嗜热菌海栖热袍菌的CheA组氨酸激酶的亚基交换
Biochemistry. 2004 Mar 2;43(8):2228-40. doi: 10.1021/bi0352419.
9
Dehydration converts DsbG crystal diffraction from low to high resolution.脱水将DsbG晶体衍射从低分辨率转变为高分辨率。
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10
The solution structure and interactions of CheW from Thermotoga maritima.嗜热栖热菌CheW的溶液结构与相互作用
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嗜热栖热菌CheA的P3-P4-P5结构域与CheW复合物的结晶及初步X射线晶体学分析

Crystallization and preliminary X-ray crystallographic analysis of Thermotoga maritima CheA P3-P4-P5 domains in complex with CheW.

作者信息

Park Sangyoun, Kim Keon Young, Kim Sunmin, Crane Brian R

机构信息

School of Systems Biomedical Science, Soongsil University, Seoul, Republic of Korea.

出版信息

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Jun 1;68(Pt 6):713-5. doi: 10.1107/S174430911201826X. Epub 2012 May 24.

DOI:10.1107/S174430911201826X
PMID:22684078
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3370918/
Abstract

The CheA-CheW complex plays a key role in bacterial chemotaxis signal transduction by initiating phosphotransfer to response regulators via coupling to the chemoreceptors. CheA (P3-P4-P5 domains) and CheW from Thermotoga maritima were overexpressed in Escherichia coli and crystallized as a complex at 298 K using ammonium dihydrogen phosphate as a precipitant. X-ray diffraction data were collected to ~8 Å resolution at 100 K using synchrotron radiation. The crystal belonged to space group I222 or I2(1)2(1)2(1), with unit-cell parameters a = 184.2, b = 286.4, c = 327.7 Å. The asymmetric unit may contain six to ten CheA-CheW molecules.

摘要

CheA-CheW复合物通过与化学感受器偶联启动磷酸转移至应答调节因子，在细菌趋化信号转导中起关键作用。来自嗜热栖热菌的CheA（P3-P4-P5结构域）和CheW在大肠杆菌中过表达，并使用磷酸二氢铵作为沉淀剂在298 K下结晶为复合物。利用同步辐射在100 K下收集了分辨率约为8 Å的X射线衍射数据。晶体属于空间群I222或I2(1)2(1)2(1)，晶胞参数a = 184.2、b = 286.4、c = 327.7 Å。不对称单元可能包含6至10个CheA-CheW分子。