CLPB

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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.