View source for 4bzk


==The structure of the COPII coat assembled on membranes==
<SX load='4bzk' size='340' side='right' viewer='molstar' caption='[[4bzk]], [[Resolution|resolution]] 40.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4bzk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BZK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BZK 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]] 40&#8491;</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=4bzk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bzk OCA], [https://pdbe.org/4bzk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bzk RCSB], [https://www.ebi.ac.uk/pdbsum/4bzk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bzk ProSAT]</span></td></tr>
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== Function ==
[https://www.uniprot.org/uniprot/SEC31_YEAST SEC31_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.<ref>PMID:8548805</ref> <ref>PMID:8852839</ref> <ref>PMID:9190202</ref> <ref>PMID:9023343</ref> <ref>PMID:10720463</ref> <ref>PMID:14627716</ref> 
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== Publication Abstract from PubMed ==
Coat protein complex II (COPII) mediates formation of the membrane vesicles that export newly synthesised proteins from the endoplasmic reticulum. The inner COPII proteins bind to cargo and membrane, linking them to the outer COPII components that form a cage around the vesicle. Regulated flexibility in coat architecture is essential for transport of a variety of differently sized cargoes, but structural data on the assembled coat has not been available. We have used cryo-electron tomography and subtomogram averaging to determine the structure of the complete, membrane-assembled COPII coat. We describe a novel arrangement of the outer coat and find that the inner coat can assemble into regular lattices. The data reveal how coat subunits interact with one another and with the membrane, suggesting how coordinated assembly of inner and outer coats can mediate and regulate packaging of vesicles ranging from small spheres to large tubular carriers. DOI:http://dx.doi.org/10.7554/eLife.00951.001.

The structure of the COPII transport-vesicle coat assembled on membranes.,Zanetti G, Prinz S, Daum S, Meister A, Schekman R, Bacia K, Briggs JA Elife. 2013 Sep 17;2:e00951. doi: 10.7554/eLife.00951. PMID:24062940<ref>PMID:24062940</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 4bzk" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Bacia K]]
[[Category: Briggs JAG]]
[[Category: Daum S]]
[[Category: Meister A]]
[[Category: Prinz S]]
[[Category: Schekman R]]
[[Category: Zanetti G]]