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Structure paper

TitleBinding-induced folding of prokaryotic ubiquitin-like protein on the Mycobacterium proteasomal ATPase targets substrates for degradation.
Journal, issue, pagesNat. Struct. Mol. Biol., Vol. 17, Page 1352-1357, Year 2010
Publish dateMar 19, 2010 (structure data deposition date)
AuthorsWang, T. / Darwin, K.H. / Li, H.
External linksNat. Struct. Mol. Biol. / PubMed:20953180
MethodsX-ray diffraction
Resolution1.8 - 4.5 Å
Structure data

PDB-3m91:
Crystal structure of the prokaryotic ubiquitin-like protein (Pup) complexed with the amino terminal coiled coil of the Mycobacterium tuberculosis proteasomal ATPase Mpa
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-3m9b:
Crystal structure of the amino terminal coiled coil domain and the inter domain of the Mycobacterium tuberculosis proteasomal ATPase Mpa
Method: X-RAY DIFFRACTION / Resolution: 3.94 Å

PDB-3m9d:
Crystal structure of the prokaryotic ubiquintin-like protein Pup complexed with the hexameric proteasomal ATPase Mpa which includes the amino terminal coiled coil domain and the inter domain
Method: X-RAY DIFFRACTION / Resolution: 4.5 Å

PDB-3m9h:
Crystal structure of the amino terminal coiled coil domain of the Mycobacterium tuberculosis proteasomal ATPase Mpa
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • mycobacterium tuberculosis (bacteria)
KeywordsHYDROLASE REGULATOR / coil coil alpha helix / ATP-binding / Chaperone / Nucleotide-binding / Proteasome / S-nitrosylation / Virulence / Isopeptide bond / Ubl conjugation pathway / coil coil with 5 beta-strand barrel inter domain / alpha helix coil coil / 5 beta-strand barrel / four helix antiparallel bundle

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