View source for 4asw


==Structure of the complex between the N-terminal dimerisation domain of Sgt2 and the UBL domain of Get5==
<StructureSection load='4asw' size='340' side='right'caption='[[4asw]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4asw]] is a 3 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=4ASW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ASW FirstGlance]. <br>
</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=4asw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4asw OCA], [https://pdbe.org/4asw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4asw RCSB], [https://www.ebi.ac.uk/pdbsum/4asw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4asw 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 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<ref>PMID:23297211</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4asw" 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: Goldstone RM]]
[[Category: High S]]
[[Category: Isaacson RL]]
[[Category: Krysztofinska EM]]
[[Category: Murray JW]]
[[Category: Simon AC]]
[[Category: Simpson PJ]]