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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Thibault, Guillaume Sprangers, Remco Zhao, Rongmin Yudin, Jovana Wong, Philip Houry, Walid A. Tsitrin, Vladimir |
| Description | Author Affiliation: Thibault G ( One King's College Circle, Medical Sciences Building, Department of Biochemistry, University of Toronto, Toronto, ON, Canada M5S 1A8.); |
| Abstract | Clp ATPases are a unique group of ATP-dependent chaperones supporting targeted protein unfolding and degradation in concert with their respective proteases. ClpX is a representative member of these ATPases; it consists of two domains, a zinc-binding domain (ZBD) that forms dimers and a AAA+ ATP-binding domain that arranges into a hexamer. Analysis of the binding preferences of these two domains in ClpX revealed that both domains preferentially bind to hydrophobic residues but have different sequence preferences, with the AAA+ domain preferentially recognizing a wider range of specific sequences than ZBD. As part of this analysis, the binding site of the ClpX dimeric cofactor, SspB2, on ZBD in ClpX was determined by NMR and mutational analysis. The SspB C terminus was found to interact with a hydrophobic patch on the surface of ZBD. The affinity of SspB2 toward ZBD2 and the geometry of the SspB2-ZBD2 complex were investigated by using the newly developed quantitative optical biosensor method of dual polarization interferometry. The data suggest a model for the interaction between SspB2 and the ClpX hexamer. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 47 |
| Volume Number | 103 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2006-11-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Adenosine Triphosphatases Metabolism Coenzymes Endopeptidase Clp Escherichia Coli Proteins Molecular Chaperones Chemistry Genetics Amino Acid Sequence Binding Sites Carrier Proteins DNA Mutational Analysis Escherichia Coli Enzymology Models, Molecular Molecular Sequence Data Nuclear Magnetic Resonance, Biomolecular Protein Structure, Quaternary Protein Structure, Tertiary Substrate Specificity Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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