2l6j
From Proteopedia
(Difference between revisions)
| Line 2: | Line 2: | ||
<StructureSection load='2l6j' size='340' side='right' caption='[[2l6j]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='2l6j' size='340' side='right' caption='[[2l6j]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | [[2l6j]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L6J OCA]. <br> | + | <table><tr><td colspan='2'>[[2l6j]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L6J OCA]. <br> |
| - | <b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span>< | + | </td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TAH1, TAH1 YCR060W YCR60W, YCR060W, YCR60W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</td></tr> |
| - | <b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2l6j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l6j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l6j RCSB], [http://www.ebi.ac.uk/pdbsum/2l6j PDBsum]</span>< | + | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr> |
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2l6j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l6j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l6j RCSB], [http://www.ebi.ac.uk/pdbsum/2l6j PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Tah1 and Pih1 are novel Hsp90 interactors. Tah1 acts as a cofactor of Hsp90 to stabilize Pih1. In yeast, Hsp90, Tah1, and Pih1 were found to form a complex that is required for ribosomal RNA processing through their effect on box C/D snoRNP assembly. Tah1 is a minimal tetratricopeptide repeat (TPR) protein of 111 amino acid residues that binds to the C-terminus of the Hsp90 molecular chaperone, while Pih1 consists of 344 residues of unknown fold. The NMR structure of Tah1 has been solved and this structure shows the presence of two TPR motifs followed by a C helix and an unstructured region. The binding of Tah1 to Hsp90 is mediated by the EEVD C-terminal residues of Hsp90, which bind to a positively charged channel formed by Tah1. Five highly conserved residues, which form a two-carboxylate clamp that tightly interacts with the ultimate D0 residue of the bound peptide, are also present in Tah1. Tah1 was found to bind to the C-terminus of Pih1 through the C helix and the unstructured region. The C-terminus of Pih1 destabilizes the protein in vitro and in vivo, while the binding of Tah1 to Pih1 allows for the formation of a stable complex. Based on our data a model for an Hsp90-Tah1-Pih1 ternary complex is proposed. | Tah1 and Pih1 are novel Hsp90 interactors. Tah1 acts as a cofactor of Hsp90 to stabilize Pih1. In yeast, Hsp90, Tah1, and Pih1 were found to form a complex that is required for ribosomal RNA processing through their effect on box C/D snoRNP assembly. Tah1 is a minimal tetratricopeptide repeat (TPR) protein of 111 amino acid residues that binds to the C-terminus of the Hsp90 molecular chaperone, while Pih1 consists of 344 residues of unknown fold. The NMR structure of Tah1 has been solved and this structure shows the presence of two TPR motifs followed by a C helix and an unstructured region. The binding of Tah1 to Hsp90 is mediated by the EEVD C-terminal residues of Hsp90, which bind to a positively charged channel formed by Tah1. Five highly conserved residues, which form a two-carboxylate clamp that tightly interacts with the ultimate D0 residue of the bound peptide, are also present in Tah1. Tah1 was found to bind to the C-terminus of Pih1 through the C helix and the unstructured region. The C-terminus of Pih1 destabilizes the protein in vitro and in vivo, while the binding of Tah1 to Pih1 allows for the formation of a stable complex. Based on our data a model for an Hsp90-Tah1-Pih1 ternary complex is proposed. | ||
| Line 11: | Line 14: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 09:36, 1 May 2014
Tah1 complexed by MEEVD
| |||||||||||
