Crystallographic characterization of a novel protein SixA which exhibits phospho-histidine phosphatase activity in the multistep His-Asp phosphorelay.

Hamada K; Mizuno T; Hakoshima TKato M

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Crystallographic characterization of a novel protein SixA which exhibits phospho-histidine phosphatase activity in the multistep His-Asp phosphorelay.

机译：晶体特征的小说蛋白质SixA展品phospho-histidine在多步His-Asp磷酸酶活性phosphorelay。

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SixA has been isolated from Escherichia coli as the first protein to exhibit phospho-histidine phosphatase activity. Recent biochemical studies have shown that SixA is involved in the signal transduction of the His-Asp phosphorelay through the dephosphorylation of the histidine-containing phosphotransfer (HPt) domain of the anaerobic sensor kinase ArcB. Crystals of SixA were obtained using a hanging-drop vapour-diffusion method with polyethylene glycol and calcium ions. Preliminary X-ray crystallographic analysis revealed that the crystals belonged to space group P212121 with unit-cell dimensions a = 39.26, b = 48.62 and c = 83.18 A, having one molecule in the crystallographic asymmetric unit. The intensity data were collected up to 1.5 A resolution using synchrotron radiation.

机译：SixA已经从大肠杆菌分离出来第一个展览phospho-histidine蛋白质磷酸酶活性。表明SixA参与信号转导的His-Asp phosphorelay通过histidine-containing的去磷酸化厌氧的phosphotransfer (HPt)域传感器激酶ArcB。获得使用悬滴vapour-diffusion方法以聚乙二醇和钙离子。初步的x射线晶体分析表明晶体属于空间集团P212121单胞尺寸=39.26, b = 48.62和c = 83.18,一个分子晶体的不对称单元。1.5强度数据收集使用同步辐射分辨率。

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来源
《Acta crystallographica.Section D. Biological crystallography》 |1999年第1期|269-271|共3页
作者
Hamada K; Mizuno T; Hakoshima TKato M;
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作者单位

Department of Molecular Biology, Nara Institute of Science and Technology (NAIST), 8916-5 Takayama, Ikoma, Nara 630-01, Japan.;

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正文语种英语
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关键词
Crystallography; crystals; PhosphataseHistidine Metabolism PathwayCalcium CationX-raysDephosphorylationCrystallization;

机译：结晶学;晶体;PhosphataseHistidine新陈代谢PathwayCalciumCationX-raysDephosphorylationCrystallization;

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Crystallographic characterization of a novel protein SixA which exhibits phospho-histidine phosphatase activity in the multistep His-Asp phosphorelay.

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