This subproject is one of many research subprojects utilizing theresources provided by a Center grant funded by NIH/NCRR. The subproject andinvestigator (PI) may have received primary funding from another NIH source,and thus could be represented in other CRISP entries. The institution listed isfor 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.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR002250-22
Application #
7598591
Study Section
Special Emphasis Panel (ZRG1-BPC-K (40))
Project Start
2006-12-01
Project End
2007-11-30
Budget Start
2006-12-01
Budget End
2007-11-30
Support Year
22
Fiscal Year
2007
Total Cost
$16,288
Indirect Cost
Name
Baylor College of Medicine
Department
Physiology
Type
Schools of Medicine
DUNS #
051113330
City
Houston
State
TX
Country
United States
Zip Code
77030
Bucero, Marta Abril; Bajaj, Chandrajit; Mourrain, Bernard (2016) On the construction of general cubature formula by flat extensions. Linear Algebra Appl 502:104-125
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