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| | ==Solution structure of the Sgt2 homodimerization domain== | | ==Solution structure of the Sgt2 homodimerization domain== |
| - | <StructureSection load='2lxb' size='340' side='right'caption='[[2lxb]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='2lxb' size='340' side='right'caption='[[2lxb]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2lxb]] is a 2 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=2LXB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LXB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2lxb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LXB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LXB FirstGlance]. <br> |
| - | </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]], [[2lxc|2lxc]], [[4god|4god]], [[4goe|4goe]], [[4gof|4gof]]</div></td></tr> | + | </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=2lxb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lxb OCA], [https://pdbe.org/2lxb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lxb RCSB], [https://www.ebi.ac.uk/pdbsum/2lxb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lxb ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SGT2, UNF346, YOR007C ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2lxb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lxb OCA], [https://pdbe.org/2lxb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lxb RCSB], [https://www.ebi.ac.uk/pdbsum/2lxb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lxb ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == 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>
| + | [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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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Baker's yeast]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chartron, J W]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Clemons, W M]] | + | [[Category: Chartron JW]] |
| - | [[Category: Vandervelde, D G]] | + | [[Category: Clemons Jr WM]] |
| - | [[Category: Four-helix bundle]] | + | [[Category: Vandervelde DG]] |
| - | [[Category: Get pathway]]
| + | |
| - | [[Category: Get5 binding domain]]
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| - | [[Category: Protein binding]]
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| - | [[Category: Protein-protein interaction]]
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| Structural highlights
Function
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.[1]
Publication Abstract from PubMed
In 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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Angeletti PC, Walker D, Panganiban AT. Small glutamine-rich protein/viral protein U-binding protein is a novel cochaperone that affects heat shock protein 70 activity. Cell Stress Chaperones. 2002 Jul;7(3):258-68. PMID:12482202
- ↑ Chartron JW, Vandervelde DG, Clemons WM Jr. Structures of the Sgt2/SGTA Dimerization Domain with the Get5/UBL4A UBL Domain Reveal an Interaction that Forms a Conserved Dynamic Interface. Cell Rep. 2012 Nov 7. pii: S2211-1247(12)00346-4. doi:, 10.1016/j.celrep.2012.10.010. PMID:23142665 doi:http://dx.doi.org/10.1016/j.celrep.2012.10.010
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