Backbone resonance assignments of the 25kD N-terminal ATPase domain from the
Hsp90 chaperone

The system reported consists of residues 1 to 207 of the sequence entry,
plus an N-terminal hexahistidine-tag (MRGSHHHHHHG).

Conformational and solvent exchange has resulted in a number of missing peaks
in the 3D spectra and consequently there are no assignements for residues 9-11,
23-25 and 97-100.

Backbone resonance assignments of the 25kD N-terminal ATPase domain from the Hsp90 chaperone.

Pearl LH, Prodromou C.
Structure, function, and mechanism of the Hsp90 molecular chaperone.
Adv Protein Chem. 2001;59:157-86.

Structure, function, and mechanism of the Hsp90 molecular chaperone.

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.

Prodromou C, Roe SM, O'Brien R, Ladbury JE, Piper PW, Pearl LH.
Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone.
Cell. 1997 Jul 11;90(1):65-75.

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

Structure Of The N-Terminal Domain Of The Yeast Hsp90 Chaperone In Complex With Geldanamycin

Structure Of The Tetragonal Form Of The N-Terminal Domain Of The Yeast Hsp90 Chaperone

Structure Of The Orthorhombic Form Of The N-Terminal Domain Of The Yeast Hsp90 Chaperone

Atp Binding Site In The Hsp90 Molecular Chaperone

Adp Binding Site In The Hsp90 Molecular Chaperone

Radicicol Bound To The Atp Binding Site Of The N-Terminal Domain Of The Yeast Hsp90 Chaperone

Structure Of A Hsp90 Inhibitor Bound To The N-Terminus Of Yeast Hsp90.

Crystal Structure Of An Hsp90-Sba1 Closed Chaperone Complex

A Radicicol Analogue Bound To The Atp Binding Site Of The N- Terminal Domain Of The Yeast Hsp90 Chaperone

Radicicol Analogues Bound To The Atp Site Of Hsp90

Analogues Of Radicicol Bound To The Atp-Binding Site Of Hsp90

Structure Of The Hsp90 Inhibitor 7-O-Carbamoylpremacbecin Bound To The N- Terminus Of Yeast Hsp90

Structure Of The Hsp90 Inhibitor Macbecin Bound To The N- Terminus Of Yeast Hsp90

Yeast Hsp90 N-Terminal Domain Li-Iv Mutant With Adp

Yeast Hsp90 N-Terminal Domain Li-Iv Mutant With Geldanamycin

Yeast Hsp90 N-Terminal Domain Li-Iv Mutant With Radicicol

Hsp90 Complexed With A Resorcylic Acid Macrolactone.

Macrolactone Inhibitor Bound To Hsp90 N-Term

E88g-n92l Mutant Of N-term Hsp90 Complexed With Geldanamycin

L89v, L93i And V136m Mutant Of N-term Hsp90 Complexed With Geldanamycin

The Structure Of Modified Benzoquinone Ansamycins Bound To Yeast N-terminal Hsp90

Hsp90 N-terminal Domain Bound To Macrolactam Analogues Of Radicicol.

K7_Hsp82p [Saccharomyces cerevisiae Kyokai no. 7]

Hsp82p [Saccharomyces cerevisiae EC1118]

hsp82 protein [Saccharomyces cerevisiae]

Hsp82p [Saccharomyces cerevisiae YJM993]

heat shock protein 90 [Saccharomyces cerevisiae YJM789]

heat shock protein 90 [Saccharomyces cerevisiae RM11-1a]

YMR186Wp-like protein [Saccharomyces cerevisiae AWRI1631]

Hsp90 family chaperone HSP82 [Saccharomyces cerevisiae S288c]

RecName: Full=ATP-dependent molecular chaperone HSP82; AltName: Full=82 kDa heat shock protein; AltName: Full=Heat shock protei

TPA: Hsp90 family chaperone HSP82 [Saccharomyces cerevisiae S288c]

Delaglio, F., Grzesiek, S., Vuister, G.W., Pfeifer, J. and Bax, A.
J. Biomol. NMR 6, 277-293 (1995).

Grzesiek, S. and Bax, A.
J Biomol. NMR 3, 185-204 (1993).

Kraulis, P.J., Domaille, P.J., Campbell-Burke, S.L., van Aken, T. and Laue, E.D.
Biochemistry 33, 3515-3531 (1994).