MM-CPN - TYPE II CHAPERONIN

该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。次级项目的主要支助 而子项目的主要调查员可能是由其他来源提供的， 包括其它NIH来源。 列出的子项目总成本可能 表示子项目使用的中心基础设施的估计数量， 而不是由NCRR赠款提供给子项目或子项目工作人员的直接资金。 Mm-cpn是一种约1 MDa的胰岛II型伴侣蛋白。它的结构组织比较简单 比TRIC，哺乳动物II型伴侣蛋白，因为，虽然也是16聚体， 只有一个亚单位同种型。II类伴侣蛋白是细胞蛋白质的重要介质 真核生物和古细菌中的折叠。这些寡聚蛋白机器，约1 MDa，由以下组成： 两个背靠背的环，围绕容纳多肽的中心腔 印刷受体. 伴侣蛋白介导的蛋白质折叠严重依赖于蛋白质折叠的闭合。 内置的盖子，这是触发ATP水解。结构重组和 导致眼睑闭合的分子事件仍然是未知的。我们建议确定其 在近原子分辨率的不同化学状态下的结构。

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.