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Structure paper

TitleStructural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements.
Journal, issue, pagesCell(Cambridge,Mass. ), Vol. 127, Page 329-340, Year 2006
Publish dateApr 19, 2006 (structure data deposition date)
AuthorsShiau, A.K. / Harris, S.F. / Southworth, D.R. / Agard, D.A.
External linksCell(Cambridge,Mass. ) / PubMed:17055434
MethodsX-ray diffraction
Resolution1.65 - 3.55 Å
Structure data

PDB-2gq0:
Crystal Structure of the Middle Domain of HtpG, the E. coli Hsp90
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-2iop:
Crystal Structure of Full-length HtpG, the Escherichia coli Hsp90, Bound to ADP
Method: X-RAY DIFFRACTION / Resolution: 3.55 Å

PDB-2ioq:
Crystal Structure of full-length HTPG, the Escherichia coli HSP90
Method: X-RAY DIFFRACTION / Resolution: 3.5 Å

PDB-2ior:
Crystal Structure of the N-terminal Domain of HtpG, the Escherichia coli Hsp90, Bound to ADP
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

Chemicals

ChemComp-HOH:
WATER

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

ChemComp-MG:
Unknown entry

ChemComp-HEZ:
HEXANE-1,6-DIOL

Source
  • escherichia coli (E. coli)
KeywordsChaperone / hydrolase / MOLECULAR CHAPERONE / HSP90 / HTPG / E. COLI / Heat Shock Protein

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