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Structure paper

TitleCrystallographic investigation of peptide binding sites in the N-domain of the ClpA chaperone.
Journal, issue, pagesJ. Struct. Biol., Vol. 146, Page 166-179, Year 2004
Publish dateOct 15, 2003 (structure data deposition date)
AuthorsXia, D. / Esser, L. / Singh, S.K. / Guo, F. / Maurizi, M.R.
External linksJ. Struct. Biol. / PubMed:15037248
MethodsX-ray diffraction
Resolution2.15 - 2.35 Å
Structure data

PDB-1r6b:
High resolution crystal structure of ClpA
Method: X-RAY DIFFRACTION / Resolution: 2.25 Å

PDB-1r6c:
High resolution structure of ClpN
Method: X-RAY DIFFRACTION / Resolution: 2.15 Å

PDB-1r6o:
ATP-dependent Clp protease ATP-binding subunit clpA/ATP-dependent Clp protease adaptor protein clpS
Method: X-RAY DIFFRACTION / Resolution: 2.25 Å

PDB-1r6q:
ClpNS with fragments
Method: X-RAY DIFFRACTION / Resolution: 2.35 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-HOH:
WATER

ChemComp-ZN:
Unknown entry

ChemComp-YBT:
BIS-(2-HYDROXYETHYL)AMINO-TRIS(HYDROXYMETHYL)METHANE YTTRIUM

ChemComp-GOL:
GLYCEROL

ChemComp-CL:
Unknown entry

ChemComp-Y1:
YTTRIUM ION

Source
  • escherichia coli (E. coli)
KeywordsHYDROLASE / ClpA / AAA+ / N-terminal Domain / ClpS / crystal / binding mechanism / CHAPERONE/PROTEIN BINDING / CHAPERONE-PROTEIN BINDING COMPLEX

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