Summary for 1E94
| Entry DOI | 10.2210/pdb1e94/pdb |
| Related | 1DO0 1DO2 1NED |
| Descriptor | HEAT SHOCK PROTEIN HSLV, HEAT SHOCK PROTEIN HSLU, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (4 entities in total) |
| Functional Keywords | chaperone, hslvu, clpqy, aaa-atpase, atp-dependent proteolysis, proteasome |
| Biological source | ESCHERICHIA COLI More |
| Cellular location | Cytoplasm: P31059 |
| Total number of polymer chains | 6 |
| Total formula weight | 177950.02 |
| Authors | Song, H.K.,Hartmann, C.,Ravishankar, R.,Bochtler, M. (deposition date: 2000-10-07, release date: 2000-11-17, Last modification date: 2023-12-13) |
| Primary citation | Song, H.K.,Hartmann, C.,Ravishankar, R.,Bochtler, M.,Behrendt, R.,Moroder, L.,Huber, R. Mutational Studies on Hslu and its Docking Mode with Hslv Proc.Natl.Acad.Sci.USA, 97:14103-, 2000 Cited by PubMed Abstract: HslVU is an ATP-dependent prokaryotic protease complex. Despite detailed crystal and molecular structure determinations of free HslV and HslU, the mechanism of ATP-dependent peptide and protein hydrolysis remained unclear, mainly because the productive complex of HslV and HslU could not be unambiguously identified from the crystal data. In the crystalline complex, the I domains of HslU interact with HslV. Observations based on electron microscopy data were interpreted in the light of the crystal structure to indicate an alternative mode of association with the intermediate domains away from HslV. By generation and analysis of two dozen HslU mutants, we find that the amidolytic and caseinolytic activities of HslVU are quite robust to mutations on both alternative docking surfaces on HslU. In contrast, HslVU activity against the maltose-binding protein-SulA fusion protein depends on the presence of the I domain and is also sensitive to mutations in the N-terminal and C-terminal domains of HslU. Mutational studies around the hexameric pore of HslU seem to show that it is involved in the recognition/translocation of maltose-binding protein-SulA but not of chromogenic small substrates and casein. ATP-binding site mutations, among other things, confirm the essential role of the "sensor arginine" (R393) and the "arginine finger" (R325) in the ATPase action of HslU and demonstrate an important role for E321. Additionally, we report a better refined structure of the HslVU complex crystallized along with resorufin-labeled casein. PubMed: 11114186DOI: 10.1073/PNAS.250491797 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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