4gof: Difference between revisions
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[[ | ==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=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4gof]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4goc|4goc]], [[4god|4god]], [[4goe|4goe]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SGT, SGT1, SGTA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4gof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gof OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gof RCSB], [http://www.ebi.ac.uk/pdbsum/4gof PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:23142665</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Chartron, J W | [[Category: Chartron, J W]] | ||
[[Category: Clemons, W M | [[Category: Clemons, W M]] | ||
[[Category: VanderVelde, D G | [[Category: VanderVelde, D G]] | ||
[[Category: Four-helix bundle]] | [[Category: Four-helix bundle]] | ||
[[Category: Protein binding]] | [[Category: Protein binding]] | ||
[[Category: Protein-protein interaction]] | [[Category: Protein-protein interaction]] | ||
[[Category: Ubl4a ubiquitin-like domain]] | [[Category: Ubl4a ubiquitin-like domain]] | ||
Revision as of 12:39, 10 December 2014
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
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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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