CLPB

本子项目是利用由NIH/NCRR资助的中心赠款提供的资源的众多研究子项目之一。子项目和研究者（PI）可能已经从另一个NIH来源获得了主要资金，因此可以在其他CRISP条目中表示。列出的机构是中心的，不一定是研究者的机构。ClpB是一种依赖atp的分子机器，形成600 kda的六聚体环状结构，属于AAA+蛋白的Clp/Hsp100家族。然而，与其他分子伴侣不同，ClpB既不促进蛋白质的正向折叠，也不阻止蛋白质的聚集。相反，ClpB具有将应激损伤蛋白从聚集状态中拯救出来的非凡能力；耐热性：对诱导耐热性至关重要的功能我们最近利用电子冷冻显微镜解决了amppnp结合状态下ClpB的3.0¿分辨率晶体结构和生理组装的~21¿分辨率结构。Lee et al. (2003) Cell 115, 229-240。我们目前的目标是以更高的分辨率确定ClpB六聚体的结构，这将使我们能够更详细地描述活性状态下亚基之间的分子相互作用。

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. ClpB is an ATP-dependent molecular machine, which forms a 600-kDa hexameric ring structure and belongs to the Clp/Hsp100 family of AAA+ proteins. Unlike other molecular chaperones, however, ClpB neither promotes the forward folding nor prevents the aggregation of proteins. Instead, ClpB has the remarkable ability to rescue stress-damaged proteins from an aggregated state; a function that is essential for induced thermotolerance. We have recently solved the 3.0 ¿ resolution crystal structure of ClpB in the AMPPNP-bound state and the ~21 ¿ resolution structure of the physiological assembly using electron cryo-microscopy Lee et al. (2003) Cell 115, 229-240. Our current goal is to determine the structure of the ClpB hexamer at higher resolution, which will allow us to describe in finer detail the molecular interactions between subunits in its active state.