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| | ==Solution structure of the N-terminal dimerisation domain of Sgt2== | | ==Solution structure of the N-terminal dimerisation domain of Sgt2== |
| - | <StructureSection load='4asv' size='340' side='right'caption='[[4asv]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='4asv' size='340' side='right'caption='[[4asv]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4asv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ASV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ASV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4asv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ASV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ASV 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;'>[[4asw|4asw]], [[4as0|4as0]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=4asv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4asv OCA], [https://pdbe.org/4asv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4asv RCSB], [https://www.ebi.ac.uk/pdbsum/4asv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4asv ProSAT]</span></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=4asv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4asv OCA], [https://pdbe.org/4asv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4asv RCSB], [https://www.ebi.ac.uk/pdbsum/4asv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4asv 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: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Goldstone, R M]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: High, S]] | + | [[Category: Goldstone RM]] |
| - | [[Category: Isaacson, R L]] | + | [[Category: High S]] |
| - | [[Category: Krysztofinska, E M]] | + | [[Category: Isaacson RL]] |
| - | [[Category: Murray, J W]] | + | [[Category: Krysztofinska EM]] |
| - | [[Category: Simon, A C]] | + | [[Category: Murray JW]] |
| - | [[Category: Simpson, P J]] | + | [[Category: Simon AC]] |
| - | [[Category: Chaperone]]
| + | [[Category: Simpson PJ]] |
| - | [[Category: Membrane]]
| + | |
| - | [[Category: Post-translational targeting]]
| + | |
| - | [[Category: Tail-anchored]]
| + | |
| 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
Small, glutamine-rich, tetratricopeptide repeat protein 2 (Sgt2) is the first known port of call for many newly synthesized tail-anchored (TA) proteins released from the ribosome and destined for the GET (Guided Entry of TA proteins) pathway. This leads them to the residential membrane of the endoplasmic reticulum via an alternative to the cotranslational, signal recognition particle-dependent mechanism that their topology denies them. In yeast, the first stage of the GET pathway involves Sgt2 passing TA proteins on to the Get4/Get5 complex through a direct interaction between the N-terminal (NT) domain of Sgt2 and the ubiquitin-like (UBL) domain of Get5. Here we characterize this interaction at a molecular level by solving both a solution structure of Sgt2_NT, which adopts a unique helical fold, and a crystal structure of the Get5_UBL. Furthermore, using reciprocal chemical shift perturbation data and experimental restraints, we solve a structure of the Sgt2_NT/Get5_UBL complex, validate it via site-directed mutagenesis, and empirically determine its stoichiometry using relaxation experiments and isothermal titration calorimetry. Taken together, these data provide detailed structural information about the interaction between two key players in the coordinated delivery of TA protein substrates into the GET pathway.
Structure of the Sgt2/Get5 complex provides insights into GET-mediated targeting of tail-anchored membrane proteins.,Simon AC, Simpson PJ, Goldstone RM, Krysztofinska EM, Murray JW, High S, Isaacson RL Proc Natl Acad Sci U S A. 2013 Jan 22;110(4):1327-32. doi:, 10.1073/pnas.1207518110. Epub 2013 Jan 7. PMID:23297211[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
- ↑ Simon AC, Simpson PJ, Goldstone RM, Krysztofinska EM, Murray JW, High S, Isaacson RL. Structure of the Sgt2/Get5 complex provides insights into GET-mediated targeting of tail-anchored membrane proteins. Proc Natl Acad Sci U S A. 2013 Jan 22;110(4):1327-32. doi:, 10.1073/pnas.1207518110. Epub 2013 Jan 7. PMID:23297211 doi:http://dx.doi.org/10.1073/pnas.1207518110
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