› 2lsu

Solution NMR

The NMR high resolution structure of yeast Tah1 in a free form

Released:
DOI: 10.2210/pdb2lsu/pdb
PDB entry 2lsu coloured by chain, ensemble of 20 models, front view.
PDB entry 2lsu coloured by chain, ensemble of 20 models, side view.
PDB entry 2lsu coloured by chain, ensemble of 20 models, top view.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
High-resolution structural analysis shows how Tah1 tethers Hsp90 to the R2TP complex.
Back R, Dominguez C, Rothé B, Bobo C, Beaufils C, Moréra S, Meyer P, Charpentier B, Branlant C, Allain FH, Manival X
Structure 21 1834-47 (2013)
PMID: 24012479

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150530 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
TPR repeat-containing protein associated with Hsp90 Chain: A
Molecule details ›
Chain: A
Length: 110 amino acids
Theoretical weight: 12.39 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P25638 (Residues: 2-111; Coverage: 99%)
Gene names: TAH1, YCR060W, YCR60W
Sequence domains: Tetratricopeptide repeat
Structure domains: Tetratricopeptide repeat domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 74%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Substrate recognition and function of the R2TP complex in response to cellular stress.
von Morgen et al. (2015)
5 more

2 mentions without citation

Tah1 helix-swap dimerization prevents mixed Hsp90 co-chaperone complexes.
Morgan et al. (2015)
1 more