STRUCTURE OF PROTEIN TRANSLOCATION COMPONENTS

该子项目是利用 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得主要资金， 因此可以在其他CRISP条目中表示。列出的机构是 中心，不一定是研究者的机构。 本项目旨在确定蛋白质转运组分的晶体结构。该项目的目标是深入了解蛋白质通过膜移动的机制。为此，我们试图获得通道本身的结构、与其伴侣（ATP酶SecA、核糖体或Sec 62/63 p复合物）结合的通道的结构以及与移位多肽链作用的通道的结构。在过去，我们已经确定了结构的蛋白质易位通道，SecY复合物，从古细菌，以及结构的ATP酶SecA绑定到SecY通道。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. This project aims at determining crystal structures of protein translocation components. The goal of the project is to get insight into the mechanism by which proteins are moved through the membrane. To this end, we are trying to get structures of the channel on its own, of the channel bound to its partners (the ATPase SecA, the ribosome, or the Sec62/63p complex), and of the channel in action with a translocating polypeptide chain. In the past, we have determined the structures of the protein translocation channel, the SecY complex, from an archaebacterium, as well as the structures of the ATPase SecA bound to the SecY channel.