MM-CPN - TYPE II CHAPERONIN

MM-CPN - II 型伴侣蛋白

• 批准号: 8361101
• 负责人: JUDITH FRYDMAN
• 金额: $ 6.13万
• 依托单位: BAYLOR COLLEGE OF MEDICINE
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-01-01 至 2011-12-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8361101
• 关键词: ATP Hydrolysis; Archaea; Back; Chemicals; Electron Microscopy; Eukaryota; Event; Funding; Grant; Mediating; Mediator of activation protein; National Center for Research Resources; Principal Investigator; Protein Isoforms; Proteins; Research; Research Infrastructure; Resolution; Resources; Source; Structure; United States National Institutes of Health; chaperonin; cost; macromolecule; molecular rearrangement; polypeptide; protein folding

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.

该副本是利用资源的众多研究子项目之一 由NIH/NCRR资助的中心赠款提供。对该子弹的主要支持 而且，副投影的主要研究员可能是其他来源提供的 包括其他NIH来源。 列出的总费用可能 代表subproject使用的中心基础架构的估计量， NCRR赠款不直接向子弹或副本人员提供的直接资金。 MM-CPN是〜1 MDA的古细菌II型伴侣蛋白。它的结构组织更简单 而不是tric，哺乳动物II型伴侣蛋白，因为，虽然也有16mer 只有一个亚基同工型。第二组伴侣蛋白是细胞蛋白的必要介体 折叠真核生物和古细菌。这些寡聚蛋白机，〜1MDA，由 两个背靠背的环，包括可容纳多肽的中央空腔 基材。 伴侣蛋白介导的蛋白质折叠取决于闭合 内置盖子，由ATP水解触发。结构重排和 导致盖子闭合的分子事件仍然未知。我们建议确定其 不同化学状态的结构接近原子分辨率。