4gof: Difference between revisions
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==Crystal structure of the SGTA homodimerization domain with covalent modifications to both C38== | ==Crystal structure of the SGTA homodimerization domain with covalent modifications to both C38== | ||
<StructureSection load='4gof' size='340' side='right' caption='[[4gof]], [[Resolution|resolution]] 1.35Å' scene=''> | <StructureSection load='4gof' size='340' side='right'caption='[[4gof]], [[Resolution|resolution]] 1.35Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4gof]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4gof]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GOF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GOF FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=4gof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gof OCA], [https://pdbe.org/4gof PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gof RCSB], [https://www.ebi.ac.uk/pdbsum/4gof PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gof ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/SGTA_HUMAN SGTA_HUMAN] Co-chaperone that binds directly to HSC70 and HSP70 and regulates their ATPase activity.<ref>PMID:18759457</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 4gof" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4gof" 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/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Chartron JW]] | ||
[[Category: | [[Category: Clemons Jr WM]] | ||
[[Category: | [[Category: VanderVelde DG]] | ||
Latest revision as of 10:07, 26 October 2022
Crystal structure of the SGTA homodimerization domain with covalent modifications to both C38Crystal structure of the SGTA homodimerization domain with covalent modifications to both C38
Structural highlights
FunctionSGTA_HUMAN Co-chaperone that binds directly to HSC70 and HSP70 and regulates their ATPase activity.[1] 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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