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Structure paper

TitleStructure of the N-terminal domain of ClpC1 in complex with the antituberculosis natural product ecumicin reveals unique binding interactions.
Journal, issue, pagesActa Crystallogr D Struct Biol, Vol. 76, Page 458-471, Year 2020
Publish dateJun 13, 2019 (structure data deposition date)
AuthorsWolf, N.M. / Lee, H. / Zagal, D. / Nam, J.W. / Oh, D.C. / Suh, J.W. / Pauli, G.F. / Cho, S. / Abad-Zapatero, C.
External linksActa Crystallogr D Struct Biol / PubMed:32355042
MethodsX-ray diffraction
Resolution1.6 - 2.5 Å
Structure data

PDB-6pba:
Structure of ClpC1-NTD
Method: X-RAY DIFFRACTION / Resolution: 1.77 Å

PDB-6pbq:
Structure of ClpC1-NTD
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-6pbs:
Structure of ClpC1-NTD in complex with Ecumicin
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-6ucr:
Structure of ClpC1-NTD L92S L96P
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-PO4:
PHOSPHATE ION

ChemComp-EPE:
4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID / pH buffer*YM

ChemComp-ACT:
ACETATE ION

Source
  • mycobacterium tuberculosis (bacteria)
  • nonomuraea sp. mjm5123 (bacteria)
  • mycobacterium tuberculosis h37rv (bacteria)
KeywordsCHAPERONE / ClpC1-NTD / ATPase / Clp protease / Ecumicin / Mycobacterium tuberculosis / CHAPERONE/ANTIBIOTIC / CHAPERONE-ANTIBIOTIC complex

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