PDBsum entry: 1amw

Chaperone

PDB-id: 1amw

Asymmetric unit

Contents

Description

Header details

Header records

References

PROCHECK

Protein chain

213 a.a. *

Ligands

ADP

Waters ×344

* Residue conservation analysis

Tools

Clefts Calculation

Biological unit, dimer
- as defined in PDB file (see also PQS)

PDB id:

1amw

Name:

Chaperone

Title:

Adp binding site in the hsp90 molecular chaperone

Structure:

Heat shock protein 90. Chain: a. Fragment: n-terminal residues. Synonym: hsp90. Engineered: yes. Other_details: adp complex

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biological unit:

Dimer (from PDB file)

UniProt:

P02829 (HSP82_YEAST)

Seq:

Struc:

Seq:

Struc:

Seq:

709 a.a.

Struc:

213 a.a.

Key:	PfamA domain
Secondary structure	CATH domain

Resolution:

1.85Å

R-factor:

0.181

Authors:

L.H.Pearl,S.M.Roe,C.Prodromou

Key ref:

C.Prodromou et al. (1997). Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone.. Cell, 90, 65-75. [PubMed id: 9230303] [DOI: 10.1016/S0092-8674(00)80314-1]

Date:

19-Jun-97

Release date:

24-Jun-98

Quick_links

Procheck

Clefts

Surface

Key reference

DOI no: 10.1016/S0092-8674(00)80314-1

Cell 90:65-75 (1997)

PubMed id: 9230303

Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone.

C.Prodromou, S.M.Roe, R.O'Brien, J.E.Ladbury, P.W.Piper, L.H.Pearl.

ABSTRACT

Hsp90 molecular chaperones in eukaryotic cells play essential roles in the folding and activation of a range of client proteins involved in cell cycle regulation, steroid hormone responsiveness, and signal transduction. The biochemical mechanism of Hsp90 is poorly understood, and the involvement of ATP in particular is controversial. Crystal structures of complexes between the N-terminal domain of the yeast Hsp90 chaperone and ADP/ATP unambiguously identify a specific adenine nucleotide binding site homologous to the ATP-binding site of DNA gyrase B. This site is the same as that identified for the antitumor agent geldanamycin, suggesting that geldanamycin acts by blocking the binding of nucleotides to Hsp90 and not the binding of incompletely folded client polypeptides as previously suggested. These results finally resolve the question of the direct involvement of ATP in Hsp90 function.

Selected figure(s)

Figure 3.
Figure 3. Comparison of Bound Nucleotide Conformations in Hsc70 and Hsp90Conformations of ADP bound to (a) Hsc70 ([13]) and (b) Hsp90. The N1, N6, which make specific contacts in the ADP/ATP-binding pocket, are indicated, as is the adenine base C8 atom, which is unhindered in the Hsc70-bound conformation but hindered in the Hsp90-bound conformation.

Figure 6.

The above figures are reprinted by permission from Cell Press: Cell (1997, 90, 65-75) copyright 1997.

Figures were selected by an automated process.