MM-CPN - TYPE II CHAPERONIN

该子项目是利用资源的众多研究子项目之一 由 NIH/NCRR 资助的中心拨款提供。子项目的主要支持 并且子项目的主要研究者可能是由其他来源提供的， 包括其他 NIH 来源。 子项目可能列出的总成本 代表子项目使用的中心基础设施的估计数量， NCRR 赠款不直接向子项目或子项目工作人员提供资金。 Mm-cpn 是一种约 1 MDa 的古菌 II 型伴侣蛋白。其结构组织较为简单 与 TRIC（哺乳动物 II 型伴侣蛋白）相比，因为虽然也是 16mer，但它具有 只有一个亚基亚型。 II 组伴侣蛋白是细胞蛋白的重要介质 真核生物和古细菌中的折叠。这些寡聚蛋白质机器，〜1MDa，由 两个背对背的环包围着容纳多肽的中央空腔 基材。 伴侣蛋白介导的蛋白质折叠关键取决于 内置盖子，由 ATP 水解触发。结构调整和 导致眼睑闭合的分子事件仍然未知。我们建议确定其 以接近原子分辨率的不同化学状态的结构。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. Mm-cpn is an Archaeal type II chaperonin of ~1 MDa. Its structural organization is simpler than TRIC, the mammalian type II chaperonin, because, while also a 16mer, it possesses only a single subunit isoform. Group II chaperonins are essential mediators of cellular protein folding in eukaryotes and archaea. These oligomeric protein machines, ~1MDa, consist of two back-to-back rings encompassing a central cavity that accommodates polypeptide substrates. Chaperonin-mediated protein folding is critically dependent on the closure of a built-in lid, which is triggered by ATP hydrolysis. The structural rearrangements and molecular events leading to lid closure are still unknown. We propose to determine its structures in different chemical states at near atomic resolution.