MM-CPN - TYPE II CHAPERONIN

这个子项目是利用资源的许多研究子项目之一。 由NIH/NCRR资助的中心拨款提供。对子项目的主要支持 子项目的首席调查员可能是由其他来源提供的， 包括美国国立卫生研究院的其他来源。为子项目列出的总成本可能 表示该子项目使用的中心基础设施的估计数量， 不是由NCRR赠款提供给次级项目或次级项目工作人员的直接资金。 MM-cpn是一种古生型~1丙二醛的伴侣蛋白。它的结构组织更简单 比哺乳动物的II型伴侣蛋白TIC更重要，因为它虽然也是16聚体，但拥有 只有一个亚基亚基亚型。第二组伴侣蛋白是细胞蛋白质的重要介体 真核生物和古生物中的折叠。这些寡聚蛋白质机器，~1MDA，包括 两个背靠背的环，围绕着一个容纳多肽的中央空腔 底物。伴侣蛋白介导的蛋白质折叠在很大程度上取决于 内置盖子，由三磷酸腺苷水解触发。结构调整和 导致盖子关闭的分子事件仍然未知。我们建议确定其 近原子分辨率下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.