6zga

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "6zga" [edit=sysop:move=sysop])
Current revision (09:20, 9 April 2025) (edit) (undo)
 
(2 intermediate revisions not shown.)
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 6zga is ON HOLD
+
==COPII on membranes, inner coat==
 +
<StructureSection load='6zga' size='340' side='right'caption='[[6zga]], [[Resolution|resolution]] 4.60&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[6zga]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZGA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZGA FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.6&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=6zga FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zga OCA], [https://pdbe.org/6zga PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zga RCSB], [https://www.ebi.ac.uk/pdbsum/6zga PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zga ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/SEC23_YEAST SEC23_YEAST] Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. SEC23 interacts with BET3 in order to target TRAPPI complex to COPII involved in internalisation of plasma membrane proteins like the maltose transporter.<ref>PMID:2670558</ref> <ref>PMID:6996832</ref> <ref>PMID:7026045</ref> <ref>PMID:3293799</ref> <ref>PMID:3049622</ref> <ref>PMID:2188733</ref> <ref>PMID:1498369</ref> <ref>PMID:7925484</ref> <ref>PMID:8451644</ref> <ref>PMID:8548805</ref> <ref>PMID:8909535</ref> <ref>PMID:9427388</ref> <ref>PMID:9023343</ref> <ref>PMID:9624457</ref> <ref>PMID:9428766</ref> <ref>PMID:10198022</ref> <ref>PMID:11086000</ref> <ref>PMID:10720463</ref> <ref>PMID:12941276</ref> <ref>PMID:14627716</ref> <ref>PMID:16269340</ref> <ref>PMID:17287728</ref>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
COPII mediates Endoplasmic Reticulum to Golgi trafficking of thousands of cargoes. Five essential proteins assemble into a two-layer architecture, with the inner layer thought to regulate coat assembly and cargo recruitment, and the outer coat forming cages assumed to scaffold membrane curvature. Here we visualise the complete, membrane-assembled COPII coat by cryo-electron tomography and subtomogram averaging, revealing the full network of interactions within and between coat layers. We demonstrate the physiological importance of these interactions using genetic and biochemical approaches. Mutagenesis reveals that the inner coat alone can provide membrane remodelling function, with organisational input from the outer coat. These functional roles for the inner and outer coats significantly move away from the current paradigm, which posits membrane curvature derives primarily from the outer coat. We suggest these interactions collectively contribute to coat organisation and membrane curvature, providing a structural framework to understand regulatory mechanisms of COPII trafficking and secretion.
-
Authors:
+
Structure of the complete, membrane-assembled COPII coat reveals a complex interaction network.,Hutchings J, Stancheva VG, Brown NR, Cheung ACM, Miller EA, Zanetti G Nat Commun. 2021 Apr 1;12(1):2034. doi: 10.1038/s41467-021-22110-6. PMID:33795673<ref>PMID:33795673</ref>
-
Description:
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
[[Category: Unreleased Structures]]
+
</div>
 +
<div class="pdbe-citations 6zga" style="background-color:#fffaf0;"></div>
 +
 
 +
==See Also==
 +
*[[GTP-binding protein 3D structures|GTP-binding protein 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
 +
[[Category: Saccharomyces cerevisiae]]
 +
[[Category: Saccharomyces cerevisiae S288C]]
 +
[[Category: Cheung ACM]]
 +
[[Category: Hutchings J]]
 +
[[Category: Zanetti G]]

Current revision

COPII on membranes, inner coat

PDB ID 6zga

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6zga"
Personal tools