2lxc: Difference between revisions
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==Solution structure of the complex between the Sgt2 homodimerization domain and the Get5 UBL domain== | ==Solution structure of the complex between the Sgt2 homodimerization domain and the Get5 UBL domain== | ||
<StructureSection load='2lxc' size='340' side='right' caption='[[2lxc]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | <StructureSection load='2lxc' size='340' side='right'caption='[[2lxc]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2lxc]] is a 3 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2lxc]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LXC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LXC FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4goc|4goc]], [[2lxa|2lxa]], [[2lxb|2lxb]], [[4god|4god]], [[4goe|4goe]], [[4gof|4gof]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4goc|4goc]], [[2lxa|2lxa]], [[2lxb|2lxb]], [[4god|4god]], [[4goe|4goe]], [[4gof|4gof]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GET5, MDY2, TMA24, YOL111C ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GET5, MDY2, TMA24, YOL111C ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), SGT2, UNF346, YOR007C ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2lxc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lxc OCA], [https://pdbe.org/2lxc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lxc RCSB], [https://www.ebi.ac.uk/pdbsum/2lxc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lxc ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/MDY2_YEAST MDY2_YEAST]] Required for efficient mating. Involved in the production of alpha-factor, the KAR9 and TUB1 location to the shmoo tip and nuclear migration into pheromone-induced shmoos.<ref>PMID:10514570</ref> <ref>PMID:16390866</ref> [[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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 2lxc" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2lxc" 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 == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Baker's yeast]] | [[Category: Baker's yeast]] | ||
[[Category: Large Structures]] | |||
[[Category: Chartron, J W]] | [[Category: Chartron, J W]] | ||
[[Category: Clemons, W M]] | [[Category: Clemons, W M]] | ||
Revision as of 13:55, 19 May 2021
Solution structure of the complex between the Sgt2 homodimerization domain and the Get5 UBL domainSolution structure of the complex between the Sgt2 homodimerization domain and the Get5 UBL domain
Structural highlights
Function[MDY2_YEAST] Required for efficient mating. Involved in the production of alpha-factor, the KAR9 and TUB1 location to the shmoo tip and nuclear migration into pheromone-induced shmoos.[1] [2] [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.[3] Publication Abstract from PubMedIn the cytoplasm, the correct delivery of membrane proteins is an essential and highly regulated process. The posttranslational targeting of the important tail-anchor membrane (TA) proteins has recently been under intense investigation. A specialized pathway, called the guided entry of TA proteins (GET) pathway in yeast and the transmembrane domain recognition complex (TRC) pathway in vertebrates, recognizes endoplasmic-reticulum-targeted TA proteins and delivers them through a complex series of handoffs. An early step is the formation of a complex between Sgt2/SGTA, a cochaperone with a presumed ubiquitin-like-binding domain (UBD), and Get5/UBL4A, a ubiquitin-like domain (UBL)-containing protein. We structurally characterize this UBD/UBL interaction for both yeast and human proteins. This characterization is supported by biophysical studies that demonstrate that complex formation is mediated by electrostatics, generating an interface that has high-affinity with rapid kinetics. In total, this work provides a refined model of the interplay of Sgt2 homologs in TA targeting. Structures of the Sgt2/SGTA Dimerization Domain with the Get5/UBL4A UBL Domain Reveal an Interaction that Forms a Conserved Dynamic Interface.,Chartron JW, Vandervelde DG, Clemons WM Jr Cell Rep. 2012 Nov 7. pii: S2211-1247(12)00346-4. doi:, 10.1016/j.celrep.2012.10.010. PMID:23142665[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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