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Structure paper

TitleStructural basis for the assembly and gate closure mechanisms of the Mycobacterium tuberculosis 20S proteasome.
Journal, issue, pagesEmbo J., Year 2010
Publish dateApr 2, 2010 (structure data deposition date)
AuthorsLi, D. / Li, H. / Wang, T. / Pan, H. / Lin, G.
External linksEmbo J. / PubMed:20461058
MethodsX-ray diffraction
Resolution2.2 - 2.6 Å
Structure data

PDB-3mfe:
Crystal Structure of Mycobacterium Tuberculosis Proteasome open-gate mutant with H0 movement
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-3mi0:
Crystal Structure of Mycobacterium Tuberculosis Proteasome at 2.2 A
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-3mka:
Crystal Structure of Mycobacterium Tuberculosis Proteasome with propetide and an T1A mutation at beta-subunit
Method: X-RAY DIFFRACTION / Resolution: 2.51 Å

Chemicals

ChemComp-HOH:
WATER / Water

ChemComp-DMF:
DIMETHYLFORMAMIDE / Dimethylformamide

ChemComp-SA6:
(2R,3S,4R)-2-[(S)-(1S)-cyclohex-2-en-1-yl(hydroxy)methyl]-4-ethyl-3-hydroxy-3-methyl-5-oxopyrrolidine-2-carbaldehyde

Source
  • mycobacterium tuberculosis (bacteria)
KeywordsHYDROLASE / Catalytic Domain / Hydrogen Bonding / Mycobacterium tuberculosis / Oxazolidinones / Protease Inhibitors / Proteasome Endopeptidase Complex / Protein Carbonylation / Protein Conformation / Protein Subunits / Substrate Specificity / Thiazoles / helix movement / Enzyme Inhibitors / Lactones / Propeptide / Protein maturation / Proteasome Assembly

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