2LSU

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

Summary for 2LSU

• Entry DOI: 10.2210/pdb2lsu/pdb
• Related: 2LSV
• NMR Information: BMRB: 18445
• Descriptor: TPR repeat-containing protein associated with Hsp90 (1 entity in total)
• Functional Keywords: chaperone, protein binding
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Cellular location: Cytoplasm: P25638
• Total number of polymer chains: 1
• Total formula weight: 12392.94

Authors

Back, R.,Dominguez, C.,Rothe, B.,Bobo, C.,Beaufils, C.,Morera, S.,Meyer, P.,Charpentier, B.,Branlant, C.,Allain, F.,Manival, X. (deposition date: 2012-05-07, release date: 2013-05-22, Last modification date: 2024-05-15)

Primary citation

Back, R.,Dominguez, C.,Rothe, B.,Bobo, C.,Beaufils, C.,Morera, S.,Meyer, P.,Charpentier, B.,Branlant, C.,Allain, F.H.,Manival, X.
High-Resolution Structural Analysis Shows How Tah1 Tethers Hsp90 to the R2TP Complex.
Structure, 21:1834-1847, 2013

PubMed Abstract: 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.

PubMed: 24012479
DOI: 10.1016/j.str.2013.07.024

Experimental method

SOLUTION NMR