5lyp: Difference between revisions

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OCA

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-'''Unreleased structure'''
-The entry 5lyp is ON HOLD
+==Crystal structure of the Tpr Domain of Sgt2.==
+<StructureSection load='5lyp' size='340' side='right'caption='[[5lyp]], [[Resolution|resolution]] 1.55&Aring;' 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]] 1.55&#8491;</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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</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]]