3MFE

Crystal Structure of Mycobacterium Tuberculosis Proteasome open-gate mutant with H0 movement

Summary for 3MFE

• Entry DOI: 10.2210/pdb3mfe/pdb
• Related: 3FHA
• Descriptor: Proteasome subunit beta, Proteasome subunit alpha, ... (4 entities in total)
• Functional Keywords: catalytic domain, hydrogen bonding, mycobacterium tuberculosis, oxazolidinones, protease inhibitors, proteasome endopeptidase complex, protein carbonylation, protein conformation, protein subunits, substrate specificity, thiazoles, helix movement, hydrolase
• Biological source: Mycobacterium tuberculosis; More
• Cellular location: Cytoplasm (By similarity): O33245 O33245 O33244
• Total number of polymer chains: 28
• Total formula weight: 717759.27

Authors

Li, D.,Li, H. (deposition date: 2010-04-02, release date: 2010-06-23, Last modification date: 2023-11-22)

Primary citation

Li, D.,Li, H.,Wang, T.,Pan, H.,Lin, G.,Li, H.
Structural basis for the assembly and gate closure mechanisms of the Mycobacterium tuberculosis 20S proteasome.
Embo J., 2010

PubMed Abstract: Mycobacterium tuberculosis (Mtb) possesses a proteasome system analogous to the eukaryotic ubiquitin-proteasome pathway. Mtb requires the proteasome to resist killing by the host immune system. The detailed assembly process and the gating mechanism of Mtb proteasome have remained unknown. Using cryo-electron microscopy and X-ray crystallography, we have obtained structures of three Mtb proteasome assembly intermediates, showing conformational changes during assembly, and explaining why the beta-subunit propeptide inhibits rather than promotes assembly. Although the eukaryotic proteasome core particles close their protein substrate entrance gates with different amino terminal peptides of the seven alpha-subunits, it has been unknown how a prokaryotic proteasome might close the gate at the symmetry axis with seven identical peptides. We found in the new Mtb proteasome crystal structure that the gate is tightly sealed by the seven identical peptides taking on three distinct conformations. Our work provides the structural bases for assembly and gating mechanisms of the Mtb proteasome.

PubMed: 20461058
DOI: 10.1038/emboj.2010.95

Experimental method

X-RAY DIFFRACTION (2.6 Å)