Crystallization and preliminary X-ray analysis of the Escherichia coli adaptor protein ClpS, free and in complex with the N-terminal domain of ClpA.

Zeth K; Dougan DA; Cusack SBukau BRavelli RB

首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Crystallization and preliminary X-ray analysis of the Escherichia coli adaptor protein ClpS, free and in complex with the N-terminal domain of ClpA.

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Crystallization and preliminary X-ray analysis of the Escherichia coli adaptor protein ClpS, free and in complex with the N-terminal domain of ClpA.

机译：结晶和初步的x射线分析大肠杆菌适配器蛋白质ClpS后续免费在复杂的n端结构域ClpA。

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Protein degradation in Escherichia coli is accomplished by a handful of large oligomeric complexes. In most cases, these proteolytic machines are comprised of a chaperone (e.g. ClpA) that is required to prepare the substrate for degradation by the peptidase (e.g. ClpP). Recently, it was shown that the substrate recognition of the chaperone ClpA could be modified by the adaptor protein ClpS. To investigate the structural implications of this change in substrate specificity, ClpS was crystallized alone and in complex with the N-terminal domain of ClpA (ClpA(N)). Crystals of ClpS diffract to 2.9 A resolution and belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 82.63, b = 145.67, c = 152.31 A. Two different crystal forms of the ClpA(N)-ClpS complex were characterized. Crystal form I (CFI) belongs to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 91.63, b = 112.47, c = 38.47 A; data to 1.92 A resolution were collected. Crystals of form II (CFII) belong to space group P4(1/3)2(1)2, with unit-cell parameters a = b = 93.57, c = 78.77 A, and diffract to 1.85 A resolution. Data sets collected from heavy-atom derivatives of CFI indicated the incorporation of Pt and Hg atoms. Structure solution using MIR and MAD methods is currently under way.

机译：蛋白质在大肠杆菌降解通过为数不多的大型低聚物的复合物。机器是由一个女伴(例如ClpA)所需准备的基质退化的肽酶(例如ClpP)。最近,结果表明,底物识别的女伴ClpA由适配器蛋白质ClpS后续修改。调查的结构性影响底物特异性变化,ClpS后续结晶和复杂ClpA N端结构域(ClpA (N))。ClpS后续衍射分辨率和属于2.9空间群P2(1) 2(1) 2(1),与单胞参数= 82.63,b = 145.67, c = 152.31。两个不同的晶体形式的ClpA (N) clps后续复杂的特征。属斜方晶系的空间群P2(1) 2(1) 2,晶胞参数= 91.63,b = 112.47, c = 38.47;分辨率收集。(CFII)属于空间群P4 (1/3) 2 (1) 2,晶胞参数a = b = 93.57, c = 78.77,1.85和衍射分辨率。收集来自CFI重原子衍生物表示Pt和汞原子的结合。结构解决方案使用米尔和疯狂的方法目前正在进行。

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《Acta crystallographica.Section D. Biological crystallography》 |2002年第7期|1207-1210|共4页
作者
Zeth K; Dougan DA; Cusack SBukau BRavelli RB;
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EMBL Outstation Grenoble, 6 Rue Jules Horowitz, BP 181, 38042 Grenoble CEDEX 9, France. zeth@biochem.mpg.de;

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正文语种英语
中图分类化学;
关键词
Escherichia coli; Adenosine Triphosphatases; cell parameterCrystallographycrystalsAdaptor Signaling ProteinCrystallizationCarrier ProteinsX-ray analysisMolecular ChaperonesEscherichia coli ProteinsBinding ProteinX-rays;

机译：大肠杆菌,腺苷三磷酸酶;细胞parameterCrystallographycrystalsAdaptor信号ProteinCrystallizationCarrier ProteinsX-rayanalysisMolecular ChaperonesEscherichia杆菌ProteinsBinding ProteinX-rays;

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Crystallization and preliminary X-ray analysis of the Escherichia coli adaptor protein ClpS, free and in complex with the N-terminal domain of ClpA.

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