6PBU
ClpP1 from Mycobacterium smegmatis
Summary for 6PBU
| Entry DOI | 10.2210/pdb6pbu/pdb |
| Descriptor | ATP-dependent Clp protease proteolytic subunit, MALONATE ION (3 entities in total) |
| Functional Keywords | protease, degradation, aaa+ unfoldase, hydrolase |
| Biological source | Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155) |
| Total number of polymer chains | 7 |
| Total formula weight | 165212.42 |
| Authors | Heras, B.,Nagpal, J.,Dougan, D.A. (deposition date: 2019-06-14, release date: 2019-12-18, Last modification date: 2023-10-11) |
| Primary citation | Nagpal, J.,Paxman, J.J.,Zammit, J.E.,Alhuwaider, A.,Truscott, K.N.,Heras, B.,Dougan, D.A. Molecular and structural insights into an asymmetric proteolytic complex (ClpP1P2) from Mycobacterium smegmatis. Sci Rep, 9:18019-18019, 2019 Cited by PubMed Abstract: The ClpP protease is found in all kingdoms of life, from bacteria to humans. In general, this protease forms a homo-oligomeric complex composed of 14 identical subunits, which associates with its cognate ATPase in a symmetrical manner. Here we show that, in contrast to this general architecture, the Clp protease from Mycobacterium smegmatis (Msm) forms an asymmetric hetero-oligomeric complex ClpP1P2, which only associates with its cognate ATPase through the ClpP2 ring. Our structural and functional characterisation of this complex demonstrates that asymmetric docking of the ATPase component is controlled by both the composition of the ClpP1 hydrophobic pocket (Hp) and the presence of a unique C-terminal extension in ClpP1 that guards this Hp. Our structural analysis of ClpP1 also revealed openings in the side-walls of the inactive tetradecamer, which may represent sites for product egress. PubMed: 31792243DOI: 10.1038/s41598-019-53736-8 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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