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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Insights into the inter-ring plasticity of caseinolytic from the X-ray structure of Mycobacterium tuberculosis ClpP1
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Insights into the inter-ring plasticity of caseinolytic from the X-ray structure of Mycobacterium tuberculosis ClpP1

机译：洞察的内环可塑性caseinolytic从x射线结构结核分枝杆菌ClpP1

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摘要

Mycobacterium tuberculosis caseinolytic protease ClpP1 (Mt ClpP1) is a self-compartmentalized protease consisting of two heptameric rings stacked on top of each other, thus enclosing a catalytic chamber. Within the chamber, which can be reached through two axial pores, each of the 14 identical monomers possesses a serine protease active site. The unfolding and translocation of substrates into the chamber are mediated by associated hexameric ATPases covering the axial pores. Three crystal structures of Mt ClpP1, determined by molecular replacement, are presented in this study. Two of the models were refined to a resolution of 2.6 angstrom and the third to 3.0 angstrom. It was found that disorder in the handle domain affects the formation and configuration of the tetradecamer and results in condensed structures with larger equatorial pores when compared with ClpPs from other species. Additionally, this disorder accompanies conformational changes of the residues in the catalytic triad. The models also reveal structural differences within the N-terminal hairpin-loop domain, which possibly reflect the significant differences in amino-acid sequence between Mt ClpP1 and other ClpP homologues in this region.
机译：结核分枝杆菌caseinolytic蛋白酶self-compartmentalized ClpP1(太ClpP1)蛋白酶两个heptameric环组成堆叠在彼此之上,因此封闭催化室。通过两个轴向孔,达到每一个14相同单体具有丝氨酸蛋白酶活跃的站点。室是由基板hexameric atp酶覆盖轴有关毛孔。由分子置换在这项研究中。2.6埃分辨率和精制第三,至3.0埃。在处理域的形成和影响配置tetradecamer和结果的凝聚结构与赤道毛孔大与其他物种相比,ClpPs。此外,这种障碍伴随残留的构象变化催化三和弦。在氨基结构差异hairpin-loop域,这可能反映了在氨基酸序列上存在显著差异太ClpP1之间和其他ClpP同系物这个地区。

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