3MI0

Crystal Structure of Mycobacterium Tuberculosis Proteasome at 2.2 A

3MI0 の概要

• エントリーDOI: 10.2210/pdb3mi0/pdb
• 分子名称: Proteasome subunit alpha, Proteasome subunit beta, DIMETHYLFORMAMIDE, ... (5 entities in total)
• 機能のキーワード: enzyme inhibitors, lactones, proteasome endopeptidase complex, mycobacterium tuberculosis, hydrolase
• 由来する生物種: Mycobacterium tuberculosis; 詳細
• 細胞内の位置: Cytoplasm (By similarity): O33244 O33245
• タンパク質・核酸の鎖数: 28
• 化学式量合計: 743523.66

構造登録者

Li, D.,Li, H. (登録日: 2010-04-09, 公開日: 2010-06-23, 最終更新日: 2024-10-16)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.2 Å)