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. Co-chaperonin proteins 10 (cpn10;GroES in Escherichia coli) are ring-shaped heptameric proteins that facilitate substrate folding when in complex with cpn60 (GroEL in E. coli). Cpn10 from the hyper-thermophilic, ancient bacterium, Aquifex aeolicus (Aacpn10) has a C-terminal 25-residue extension in each monomer not found in any other cpn10 protein. Earlier in vitro work has shown that this tail is not needed for heptamer assembly or protein function. Without the tail, however, the heptamers (Aacpn10del-25) readily aggregate into fibrillar stacked rings (Luke et al., 2005). To explain this phenomenon, Wittung-Stafshede group performed binding experiments with a peptide construct of the tail to establish its specificity for Aacpn10del-25 and proposed to use cryo-EM to determine its structure.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
2P41RR002250-25
Application #
8168556
Study Section
Special Emphasis Panel (ZRG1-BCMB-T (41))
Project Start
2010-01-15
Project End
2010-12-31
Budget Start
2010-01-15
Budget End
2010-12-31
Support Year
25
Fiscal Year
2010
Total Cost
$43,000
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
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