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PDBsum entry 4cgv
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PDB id:
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Chaperone
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Title:
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First tpr of spaghetti (rpap3) bound to hsp90 peptide srmeevd
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Structure:
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RNA polymerase ii-associated protein 3. Chain: a, b, c, d. Fragment: first tpr, residues 120-255. Synonym: spaghetti. Engineered: yes. Heat shock protein hsp 90-alpha. Chain: e, f. Fragment: c-terminal peptide, residues 726-732. Synonym: heat shock 86 kda, hsp 86, hsp86, renal carcinoma antigen
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Organism_taxid: 9606
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Resolution:
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2.54Å
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R-factor:
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0.242
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R-free:
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0.267
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Authors:
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S.M.Roe,M.Pal
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Key ref:
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M.Pal
et al.
(2014).
Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1.
Structure,
22,
805-818.
PubMed id:
DOI:
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Date:
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26-Nov-13
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Release date:
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14-May-14
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PROCHECK
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Headers
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References
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Q9H6T3
(RPAP3_HUMAN) -
RNA polymerase II-associated protein 3 from Homo sapiens
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Seq:
Struc:
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665 a.a.
125 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
22:805-818
(2014)
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PubMed id:
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Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1.
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M.Pal,
M.Morgan,
S.E.Phelps,
S.M.Roe,
S.Parry-Morris,
J.A.Downs,
S.Polier,
L.H.Pearl,
C.Prodromou.
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ABSTRACT
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Client protein recruitment to the Hsp90 system depends on cochaperones that bind
the client and Hsp90 simultaneously and facilitate their interaction. Hsp90
involvement in the assembly of snoRNPs, RNA polymerases, PI3-kinase-like
kinases, and chromatin remodeling complexes depends on the TTT (Tel2-Tti1-Tti2),
and R2TP complexes-consisting of the AAA-ATPases Rvb1 and Rvb2, Tah1
(Spagh/RPAP3 in metazoa), and Pih1 (Pih1D1 in humans)-that together provide the
connection to Hsp90. The biochemistry underlying R2TP function is still poorly
understood. Pih1 in particular, at the heart of the complex, has not been
described at a structural level, nor have the multiple protein-protein
interactions it mediates been characterized. Here we present a structural and
biochemical analysis of Hsp90-Tah1-Pih1, Hsp90-Spagh, and Pih1D1-Tel2 complexes
that reveal a domain in Pih1D1 specific for binding CK2 phosphorylation sites,
and together define the structural basis by which the R2TP complex connects the
Hsp90 chaperone system to the TTT complex.
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