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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structure of Mycobacterium tuberculosis chaperonin-10 at 3.5 A resolution.
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Structure of Mycobacterium tuberculosis chaperonin-10 at 3.5 A resolution.

机译：结核分枝杆菌的结构chaperonin-10 3.5一项决议。

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摘要

Chaperonin-60 (cpn60) and chaperonin-10 (cpn10) are essential proteins involved in ATP-dependent folding of several intracellular proteins in the bacterial cell. Folding of the nascent substrate polypeptide takes place in the large central cavity formed by each ring of the tetradecameric cpn60. This large cavity is closed upon capping by the heptameric cpn10. Cpn10s interact with cpn60s primarily through a 17-residue mobile loop and regulate the release and binding of the substrate polypeptide from the cpn60 surface. Here, the structure of M. tuberculosis cpn10 is reported at 3.5 A resolution. The overall structure of the cpn10 monomer is formed of a four-stranded beta-barrel and two long stretches of highly flexible segments: the dome loop and the mobile loop. The seven subunits in the heptamer show very little conformational difference and exhibit nearly perfect sevenfold geometry. The binding sites for metal ions in the dome loop of cpn10 have been identified, suggesting the role of metal ions in the stabilization of the protein. Comparisons with the available cpn10 structures indicate several interesting features.
机译：Chaperonin-60 (cpn60)和chaperonin-10 (cpn10)蛋白质参与ATP-dependent至关重要几个胞内蛋白的折叠细菌细胞。多肽发生在大型中央空腔形成的每个tetradecameric的戒指cpn60。由heptameric cpn10。主要通过17-residue移动cpn60s循环和规范的发布和绑定从cpn60基质多肽表面。在这里,结核分枝杆菌cpn10的结构3.5一项决议。cpn10单体形成的结构四股beta-barrel和两个很长一段路高度灵活的部分:穹顶的循环循环移动。七聚物显示很少的构象差异,表现出近乎完美的7倍几何学。圆顶cpn10循环已确定,建议中金属离子的作用稳定的蛋白质。可用cpn10结构表示数有趣的特性。

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