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Structure paper

TitleStructures of ClpP in complex with acyldepsipeptide antibiotics reveal its activation mechanism
Journal, issue, pagesNat. Struct. Mol. Biol., Vol. 17, Page 471-478, Year 2010
Publish dateNov 25, 2009 (structure data deposition date)
AuthorsLee, B.-G. / Park, E.Y. / Lee, K.-E. / Jeon, H. / Sung, K.H. / Paulsen, H. / Rubsamen-Schaeff, H. / Brotz-Oesterhelt, H. / Song, H.K.
External linksNat. Struct. Mol. Biol. / PubMed:20305655
MethodsX-ray diffraction
Resolution2 - 3 Å
Structure data

PDB-3ktg:
Structure of ClpP from Bacillus subtilis in monoclinic crystal form
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-3kth:
Structure of ClpP from Bacillus subtilis in orthorombic crystal form
Method: X-RAY DIFFRACTION / Resolution: 3 Å

PDB-3kti:
Structure of ClpP in complex with ADEP1
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-3ktj:
Structure of ClpP in complex with ADEP2 in monoclinic crystal form
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-3ktk:
Structure of ClpP in complex with ADEP2 in triclinic crystal form
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

Chemicals

ChemComp-HOH:
WATER

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

ChemComp-NHE:
2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID / pH buffer*YM

Source
  • bacillus subtilis (bacteria)
  • streptococcus hawaiiensis (bacteria)
  • synthetic (others)
KeywordsHYDROLASE / ATP-binding / Nucleotide-binding / Protease / Serine protease / Stress response / HYDROLASE/ANTIBIOTIC / A54556A / enopeptin / depsipeptide / antibiotics / HYDROLASE-ANTIBIOTIC complex

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