Defining a Pathway of Communication from the C-Terminal Peptide Binding Domain to the N-Terminal ATPase Domain in a AAA Protein
| Autor: | John R Glover, Susan Lindquist, Douglas A. Hattendorf, Danielle M. Ware, Eric C. Schirmer, Melarkode S Ramakrishnan, Anil G. Cashikar |
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| Rok vydání: | 2002 |
| Předmět: |
Conformational change
Saccharomyces cerevisiae Proteins Protein Conformation ATPase Biology Mice Structure-Activity Relationship chemistry.chemical_compound Adenosine Triphosphate Protein structure Stress Physiological ATP hydrolysis Animals Polylysine Binding site Molecular Biology Antibodies Fungal Heat-Shock Proteins Adenosine Triphosphatases Binding Sites Hydrolysis Antibodies Monoclonal Cell Biology Peptide Fragments AAA proteins Protein Structure Tertiary Cell biology Enzyme Activation Amino Acid Substitution chemistry Biochemistry Mutagenesis Site-Directed biology.protein Peptides Adenosine triphosphate Binding domain |
| Zdroj: | Molecular Cell. 9:751-760 |
| ISSN: | 1097-2765 |
| DOI: | 10.1016/s1097-2765(02)00499-9 |
| Popis: | AAA proteins remodel other proteins to affect a multitude of biological processes. Their power to remodel substrates must lie in their capacity to couple substrate binding to conformational changes via cycles of nucleotide binding and hydrolysis, but these relationships have not yet been deciphered for any member. We report that when one AAA protein, Hsp104, engages polypeptide at the C-terminal peptide-binding region, the ATPase cycle of the C-terminal nucleotide-binding domain (NBD2) drives a conformational change in the middle region. This, in turn, drives ATP hydrolysis in the N-terminal ATPase domain (NBD1). This interdomain communication pathway can be blocked by mutation in the middle region or bypassed by antibodies that bind there, demonstrating the crucial role this region plays in transducing signals from one end of the molecule to the other. |
| Databáze: | OpenAIRE |
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