8A8V
| Mycobacterium tuberculosis ClpC1 hexamer structure bound to the natural product antibiotic Cyclomarin | Descriptor: | ADENOSINE-5'-DIPHOSPHATE, ATP-dependent Clp protease ATP-binding subunit ClpC1, Bound polypeptide | Authors: | Felix, J, Fraga, H, Gragera, M, Bueno, T, Weinhaeupl, K. | Deposit date: | 2022-06-24 | Release date: | 2022-10-26 | Last modified: | 2022-11-23 | Method: | ELECTRON MICROSCOPY (3.34 Å) | Cite: | Structure of the drug target ClpC1 unfoldase in action provides insights on antibiotic mechanism of action. J.Biol.Chem., 298, 2022
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8A8U
| Mycobacterium tuberculosis ClpC1 hexamer structure | Descriptor: | ADENOSINE-5'-DIPHOSPHATE, ATP-dependent Clp protease ATP-binding subunit ClpC1, Bound polypeptide | Authors: | Felix, J, Fraga, H, Gragera, M, Bueno, T, Weinhaeupl, K. | Deposit date: | 2022-06-24 | Release date: | 2022-10-26 | Last modified: | 2022-11-23 | Method: | ELECTRON MICROSCOPY (3.62 Å) | Cite: | Structure of the drug target ClpC1 unfoldase in action provides insights on antibiotic mechanism of action. J.Biol.Chem., 298, 2022
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8A8W
| Mycobacterium tuberculosis ClpC1 hexamer structure bound to the natural product antibiotic Ecumycin (class 1) | Descriptor: | ADENOSINE-5'-DIPHOSPHATE, ATP-dependent Clp protease ATP-binding subunit ClpC1, Bound polypeptide | Authors: | Felix, J, Fraga, H, Gragera, M, Bueno, T, Weinhaeupl, K. | Deposit date: | 2022-06-24 | Release date: | 2022-10-26 | Last modified: | 2022-11-23 | Method: | ELECTRON MICROSCOPY (4.29 Å) | Cite: | Structure of the drug target ClpC1 unfoldase in action provides insights on antibiotic mechanism of action. J.Biol.Chem., 298, 2022
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6HWN
| Structure of Thermus thermophilus ClpP in complex with a tripeptide. | Descriptor: | ATP-dependent Clp protease proteolytic subunit, DI(HYDROXYETHYL)ETHER, Unknown tripeptide | Authors: | Felix, J, Schanda, P, Fraga, H, Morlot, C. | Deposit date: | 2018-10-12 | Release date: | 2019-09-18 | Last modified: | 2024-01-24 | Method: | X-RAY DIFFRACTION (1.95 Å) | Cite: | Mechanism of the allosteric activation of the ClpP protease machinery by substrates and active-site inhibitors. Sci Adv, 5, 2019
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6HWM
| Structure of Thermus thermophilus ClpP in complex with bortezomib | Descriptor: | ATP-dependent Clp protease proteolytic subunit, DI(HYDROXYETHYL)ETHER, N-[(1R)-1-(DIHYDROXYBORYL)-3-METHYLBUTYL]-N-(PYRAZIN-2-YLCARBONYL)-L-PHENYLALANINAMIDE | Authors: | Felix, J, Schanda, P, Fraga, H, Morlot, C. | Deposit date: | 2018-10-12 | Release date: | 2019-09-18 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (2.7 Å) | Cite: | Mechanism of the allosteric activation of the ClpP protease machinery by substrates and active-site inhibitors. Sci Adv, 5, 2019
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