2lsu | pdb_00002lsu

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

spinqualitylabelsall models 2lsu Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2lsu is a 1 chain structure with sequence from Saccharomyces cerevisiae S288C. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TAH1_YEAST Publication Abstract from PubMed 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 704EMEEVD709 motif. In addition to Lys79 and Arg83 from the carboxylate clamp, this helix bears Tyr82 forming a pi/S-CH3 interaction with Hsp90 M705 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. High-Resolution Structural Analysis Shows How Tah1 Tethers Hsp90 to the R2TP Complex.,Back R, Dominguez C, Rothe B, Bobo C, Beaufils C, Morera S, Meyer P, Charpentier B, Branlant C, Allain FH, Manival X Structure. 2013 Sep 4. pii: S0969-2126(13)00296-7. doi:, 10.1016/j.str.2013.07.024. PMID:24012479 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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