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Structure paper

TitleCrystal structure of Mycobacterium tuberculosis ClpP1P2 suggests a model for peptidase activation by AAA+ partner binding and substrate delivery.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 111, Page E4587-E4595, Year 2014
Publish dateJul 11, 2014 (structure data deposition date)
AuthorsSchmitz, K.R. / Carney, D.W. / Sello, J.K. / Sauer, R.T.
External linksProc. Natl. Acad. Sci. USA / PubMed:25267638
MethodsX-ray diffraction
Resolution3.1978 - 3.2479 Å
Structure data

PDB-4u0g:
Crystal Structure of M. tuberculosis ClpP1P2 bound to ADEP and agonist
Method: X-RAY DIFFRACTION / Resolution: 3.1978 Å

PDB-4u0h:
Crystal Structure of M. tuberculosis ClpP1P1
Method: X-RAY DIFFRACTION / Resolution: 3.2479 Å

Chemicals

ChemComp-ZIL:
N-[(benzyloxy)carbonyl]-L-isoleucyl-L-leucine

ChemComp-SO4:
SULFATE ION

ChemComp-DMS:
DIMETHYL SULFOXIDE / DMSO, precipitant*YM

ChemComp-39Y:
(2E,5S)-5-methylhept-2-enoic acid

ChemComp-HOH:
WATER

Source
  • mycobacterium tuberculosis h37rv (bacteria)
  • synthetic construct (others)
  • mycobacterium tuberculosis (bacteria)
Keywordshydrolase/antibiotic / hydrolase / peptidase / hydrolase-antibiotic complex

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