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PDBsum entry 2lsv
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Chaperone-binding protein/chaperone
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PDB id
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2lsv
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PDB id:
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Chaperone-binding protein/chaperone
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Title:
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The nmr high resolution structure of yeast tah1 in complex with the hsp90 c-terminal tail
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Structure:
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Tpr repeat-containing protein associated with hsp90. Chain: a. Engineered: yes. Atp-dependent molecular chaperone hsp82. Chain: b. Fragment: c-terminal tail. Synonym: 82 kda heat shock protein, heat shock protein hsp90 heat- inducible isoform. Engineered: yes
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Source:
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Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 559292. Strain: atcc 204508 / s288c. Gene: tah1, ycr060w, ycr60w. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Organism_taxid: 559292
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NMR struc:
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20 models
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Authors:
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R.Back,C.Dominguez,B.Rothe,C.Bobo,C.Beaufils,S.Morera,P.Meyer, B.Charpentier,C.Branlant,F.Allain,X.Manival
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Key ref:
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R.Back
et al.
(2013).
High-resolution structural analysis shows how Tah1 tethers Hsp90 to the R2TP complex.
Structure,
21,
1834-1847.
PubMed id:
DOI:
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Date:
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07-May-12
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Release date:
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22-May-13
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PROCHECK
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Headers
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References
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P25638
(TAH1_YEAST) -
TPR repeat-containing protein associated with Hsp90 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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111 a.a.
110 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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DOI no:
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Structure
21:1834-1847
(2013)
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PubMed id:
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High-resolution structural analysis shows how Tah1 tethers Hsp90 to the R2TP complex.
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R.Back,
C.Dominguez,
B.Rothé,
C.Bobo,
C.Beaufils,
S.Moréra,
P.Meyer,
B.Charpentier,
C.Branlant,
F.H.Allain,
X.Manival.
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ABSTRACT
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The ubiquitous Hsp90 chaperone participates in snoRNP and RNA polymerase
assembly through interaction with the R2TP complex. This complex includes the
proteins Tah1, Pih1, Rvb1, and Rvb2. Tah1 bridges Hsp90 to R2TP. Its minimal TPR
domain includes two TPR motifs and a capping helix. We established the
high-resolution solution structures of Tah1 free and in complex with the Hsp90
C-terminal peptide. The TPR fold is similar in the free and bound forms and we
show experimentally that in addition to its solvating/stabilizing role, the
capping helix is essential for the recognition of the Hsp90 (704)EMEEVD(709)
motif. In addition to Lys79 and Arg83 from the carboxylate clamp, this helix
bears Tyr82 forming a π/S-CH3 interaction with Hsp90 M(705) from the peptide
310 helix. The Tah1 C-terminal region is unfolded, and we demonstrate that it is
essential for the recruitment of the Pih1 C-terminal domain and folds upon
binding.
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