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3mzl

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{{STRUCTURE_3mzl| PDB=3mzl | SCENE= }}
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==Sec13/Sec31 edge element, loop deletion mutant==
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===Sec13/Sec31 edge element, loop deletion mutant===
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<StructureSection load='3mzl' size='340' side='right' caption='[[3mzl]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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{{ABSTRACT_PUBMED_20696705}}
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3mzl]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MZL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MZL FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3mzk|3mzk]]</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ANU3, L8167.4, SEC13, YLR208W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]), D1229, SEC31, WEB1, YDL195W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</td></tr>
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<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=3mzl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mzl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mzl RCSB], [http://www.ebi.ac.uk/pdbsum/3mzl PDBsum]</span></td></tr>
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</table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mz/3mzl_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Ancestral coatomer element 1 (ACE1) proteins assemble latticework coats for COPII vesicles and the nuclear pore complex. The ACE1 protein Sec31 and Sec13 make a 2:2 tetramer that forms the edge element of the COPII outer coat. In this study, we report that the COPII accessory protein Sec16 also contains an ACE1. The 165-kD crystal structure of the central domain of Sec16 in complex with Sec13 was solved at 2.7-A resolution. Sec16 and Sec13 also make a 2:2 tetramer, another edge element for the COPII system. Domain swapping at the ACE1-ACE1 interface is observed both in the prior structure of Sec13-Sec31 and in Sec13-Sec16. A Sec31 mutant in which domain swapping is prevented adopts an unprecedented laminated structure, solved at 2.8-A resolution. Our in vivo data suggest that the ACE1 element of Sec31 can functionally replace the ACE1 element of Sec16. Our data support Sec16 as a scaffold for the COPII system and a template for the Sec13-Sec31 coat.
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==Function==
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Structure of the Sec13-Sec16 edge element, a template for assembly of the COPII vesicle coat.,Whittle JR, Schwartz TU J Cell Biol. 2010 Aug 9;190(3):347-61. PMID:20696705<ref>PMID:20696705</ref>
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[[http://www.uniprot.org/uniprot/SEC13_YEAST SEC13_YEAST]] Functions as a component of the nuclear pore complex (NPC) and the COPII coat. It is one of 5 proteins constituting the COPII coat, which is involved in anterograde (ER to Golgi) double-membrane transport vesicle formation. First the small GTPase SAR1, activated by and binding to the integral ER membrane protein SEC12, exchanges GDP for GTP and recruits the heterodimer SEC23/24, which in turn recruits the heterotetramer SEC13-SEC31. The polymerization of COPII coat complexes then causes physically the deformation (budding) of the membrane, leading to the creation of a transport vesicle. The COPII complex is dissociated upon SAR1-GTP hydrolysis to SAR1-GDP. SEC23 functions as the SAR1 GTPase activating protein, whose activity is stimulated in the presence of SEC13/31. SEC13 is directly or indirectly required for normal ER membrane and nuclear envelope morphology. It also functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. SEC13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution. Component of the SEA complex which coats the vacuolar membrane and is involved in intracellular trafficking, autophagy, response to nitrogen starvation, and amino acid biogenesis.<ref>PMID:8565072</ref> <ref>PMID:6996832</ref> <ref>PMID:7026045</ref> <ref>PMID:2188733</ref> <ref>PMID:8548805</ref> <ref>PMID:8909535</ref> <ref>PMID:9409822</ref> <ref>PMID:9199164</ref> <ref>PMID:9427388</ref> <ref>PMID:9023343</ref> <ref>PMID:10720463</ref> <ref>PMID:10747086</ref> <ref>PMID:11535824</ref> <ref>PMID:11717432</ref> <ref>PMID:12215173</ref> <ref>PMID:11823431</ref> <ref>PMID:12475940</ref> <ref>PMID:14627716</ref> <ref>PMID:21454883</ref> [[http://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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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[3mzl]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MZL OCA].
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</div>
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:020696705</ref><references group="xtra"/><references/>
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__TOC__
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</StructureSection>
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Schwartz, T U.]]
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[[Category: Schwartz, T U]]
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[[Category: Whittle, J R.]]
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[[Category: Whittle, J R]]
[[Category: Alpha-helical-stack]]
[[Category: Alpha-helical-stack]]
[[Category: Beta-propeller]]
[[Category: Beta-propeller]]
[[Category: Protein transport]]
[[Category: Protein transport]]

Revision as of 17:23, 18 December 2014

Sec13/Sec31 edge element, loop deletion mutant

3mzl, resolution 2.80Å

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