5lyp: Difference between revisions
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The | ==Crystal structure of the Tpr Domain of Sgt2.== | ||
<StructureSection load='5lyp' size='340' side='right'caption='[[5lyp]], [[Resolution|resolution]] 1.55Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5lyp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LYP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LYP FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BO4:BORATE+ION'>BO4</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5lyp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lyp OCA], [https://pdbe.org/5lyp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lyp RCSB], [https://www.ebi.ac.uk/pdbsum/5lyp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lyp ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SGT2_YEAST SGT2_YEAST] Co-chaperone that binds to the molecular chaperone Hsp70 (SSA1 and SSA2). Regulates Hsp70 ATPase activity (By similarity). Required for recovery from heat shock.<ref>PMID:12482202</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Small glutamine-rich tetratricopeptide repeat-containing protein 2 (Sgt2) is a multi-module co-chaperone involved in several protein quality control pathways. The TPR domain of Sgt2 and several other proteins, including SGTA, Hop, and CHIP, is a highly conserved motif known to form transient complexes with molecular chaperones such as Hsp70 and Hsp90. In this work, we present the first high resolution crystal structures of Sgt2_TPR alone and in complex with a C-terminal peptide PTVEEVD from heat shock protein, Ssa1. Using nuclear magnetic resonance spectroscopy and isothermal titration calorimetry, we demonstrate that Sgt2_TPR interacts with peptides corresponding to the C-termini of Ssa1, Hsc82, and Ybr137wp with similar binding modes and affinities. | |||
Structure and Interactions of the TPR Domain of Sgt2 with Yeast Chaperones and Ybr137wp.,Krysztofinska EM, Evans NJ, Thapaliya A, Murray JW, Morgan RML, Martinez-Lumbreras S, Isaacson RL Front Mol Biosci. 2017 Oct 11;4:68. doi: 10.3389/fmolb.2017.00068. eCollection, 2017. PMID:29075633<ref>PMID:29075633</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5lyp" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Small glutamine-rich tetratricopeptide repeat containing protein alpha|Small glutamine-rich tetratricopeptide repeat containing protein alpha]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Saccharomyces cerevisiae]] | |||
[[Category: Evans NJ]] | |||
[[Category: Isaacson RL]] | |||
[[Category: Krysztofinska EM]] | |||
[[Category: Martinez-Lumbreras S]] | |||
[[Category: Morgan RML]] | |||
[[Category: Murray JW]] | |||
[[Category: Thapaliya A]] | |||
Latest revision as of 13:56, 25 October 2023
Crystal structure of the Tpr Domain of Sgt2.Crystal structure of the Tpr Domain of Sgt2.
Structural highlights
FunctionSGT2_YEAST Co-chaperone that binds to the molecular chaperone Hsp70 (SSA1 and SSA2). Regulates Hsp70 ATPase activity (By similarity). Required for recovery from heat shock.[1] Publication Abstract from PubMedSmall glutamine-rich tetratricopeptide repeat-containing protein 2 (Sgt2) is a multi-module co-chaperone involved in several protein quality control pathways. The TPR domain of Sgt2 and several other proteins, including SGTA, Hop, and CHIP, is a highly conserved motif known to form transient complexes with molecular chaperones such as Hsp70 and Hsp90. In this work, we present the first high resolution crystal structures of Sgt2_TPR alone and in complex with a C-terminal peptide PTVEEVD from heat shock protein, Ssa1. Using nuclear magnetic resonance spectroscopy and isothermal titration calorimetry, we demonstrate that Sgt2_TPR interacts with peptides corresponding to the C-termini of Ssa1, Hsc82, and Ybr137wp with similar binding modes and affinities. Structure and Interactions of the TPR Domain of Sgt2 with Yeast Chaperones and Ybr137wp.,Krysztofinska EM, Evans NJ, Thapaliya A, Murray JW, Morgan RML, Martinez-Lumbreras S, Isaacson RL Front Mol Biosci. 2017 Oct 11;4:68. doi: 10.3389/fmolb.2017.00068. eCollection, 2017. PMID:29075633[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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