DETERMINING THE PATHWAY OF NASCENT-PROTEIN INSERTION THROUGH THE PROTEIN-CONDUC

确定新生蛋白通过蛋白质传导插入的途径

• 批准号: 8364332
• 负责人: Klaus Schulten
• 金额: $ 0.11万
• 依托单位: CARNEGIE-MELLON UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-09-15 至 2013-07-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8364332
• 关键词: Binding; Biomedical Research; Collaborations; Electrons; Excretory function; Funding; Grant; High Performance Computing; Ion Channel; Lateral; Membrane; National Center for Research Resources; Pathway interactions; Principal Investigator; Proteins; Research; Research Infrastructure; Resources; Ribosomes; Simulate; Source; Structure; United States National Institutes of Health; cost

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. For nascent proteins destined for excretion or membrane insertion, synthesis by the ribosome is concomitant with their insertion into a protein-conducting membrane channel, SecY, which translocates a protein across or inserts it into the membrane. In collaboration with cryo-electron microscopists we determined an all-atom structure of a ribosome-SecY-nascent-protein intermediate that permits one to investigate the membrane insertion pathway. We seek to simulate the membrane-SecY-nascent protein part of our structure to determine how the intermediate revealed, an orientationally inverted N-terminus binding outside a SecY lateral gate, arises from forces due to protein elongation.

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。 对于用于排泄或膜插入的新生蛋白质，核糖体的合成伴随着它们插入蛋白质传导膜通道 SecY，SecY 将蛋白质易位穿过膜或将其插入膜中。我们与冷冻电子显微镜专家合作，确定了核糖体-SecY-新生蛋白中间体的全原子结构，使人们能够研究膜插入途径。我们试图模拟我们结构中的膜-SecY-新生蛋白部分，以确定中间体如何揭示，即在 SecY 侧门之外的定向反向 N 末端结合，是由蛋白质伸长引起的力产生的。