2KU1
Dynamic Regulation of Archaeal Proteasome Gate Opening as Studied by TROSY-NMR
Summary for 2KU1
| Entry DOI | 10.2210/pdb2ku1/pdb |
| Related | 1PMA 1YA7 2KU2 |
| Descriptor | Proteasome subunit alpha (1 entity in total) |
| Functional Keywords | proteasome, proteolysis, gating residues, cytoplasm, hydrolase, protease, threonine protease |
| Biological source | Thermoplasma acidophilum |
| Cellular location | Cytoplasm (By similarity): P25156 |
| Total number of polymer chains | 7 |
| Total formula weight | 183020.77 |
| Authors | Religa, T.L.,Sprangers, R.,Kay, L.E. (deposition date: 2010-02-11, release date: 2010-04-21, Last modification date: 2024-05-22) |
| Primary citation | Religa, T.L.,Sprangers, R.,Kay, L.E. Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR. Science, 328:98-102, 2010 Cited by PubMed Abstract: The proteasome catalyzes the majority of protein degradation in the cell and plays an integral role in cellular homeostasis. Control over proteolysis by the 20S core-particle (CP) proteasome is achieved by gated access of substrate; thus, an understanding of the molecular mechanism by which these gates regulate substrate entry is critical. We used methyl-transverse relaxation optimized nuclear magnetic resonance spectroscopy to show that the amino-terminal residues that compose the gates of the alpha subunits of the Thermoplasma acidophilum proteasome are highly dynamic over a broad spectrum of time scales and that gating termini are in conformations that extend either well inside (closed gate) or outside (open gate) of the antechamber. Interconversion between these conformers on a time scale of seconds leads to a dynamic regulation of 20S CP proteolysis activity. PubMed: 20360109DOI: 10.1126/science.1184991 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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