3mzk

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{{STRUCTURE_3mzk| PDB=3mzk | SCENE= }}
 
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===Sec13/Sec16 complex, S.cerevisiae===
 
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{{ABSTRACT_PUBMED_20696705}}
 
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==Function==
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==Sec13/Sec16 complex, S.cerevisiae==
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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/SEC16_YEAST SEC16_YEAST]] Involved in the initiation of assembly of the COPII coat required for the formation of transport vesicles from the endoplasmic reticulum (ER) and the selection of cargo molecules. Also involved in autophagy.<ref>PMID:7593161</ref> <ref>PMID:2188733</ref> <ref>PMID:7593162</ref> <ref>PMID:9325247</ref> <ref>PMID:9023343</ref> <ref>PMID:9880808</ref> <ref>PMID:10712514</ref> <ref>PMID:11694599</ref> <ref>PMID:12235121</ref>
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<StructureSection load='3mzk' size='340' side='right'caption='[[3mzk]], [[Resolution|resolution]] 2.69&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[3mzk]] 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=3MZK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MZK FirstGlance]. <br>
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[[3mzk]] is a 4 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=3MZK OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.69&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3mzk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mzk OCA], [https://pdbe.org/3mzk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mzk RCSB], [https://www.ebi.ac.uk/pdbsum/3mzk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mzk ProSAT]</span></td></tr>
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==Reference==
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</table>
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<ref group="xtra">PMID:020696705</ref><references group="xtra"/><references/>
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== Function ==
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[https://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>
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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/3mzk_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/main_output.php?pdb_ID=3mzk ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Schwartz, T U.]]
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[[Category: Schwartz TU]]
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[[Category: Whittle, J R.]]
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[[Category: Whittle JR]]
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[[Category: Alpha-helical-stack]]
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[[Category: Beta-propeller]]
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[[Category: Protein transport]]
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Current revision

Sec13/Sec16 complex, S.cerevisiae

PDB ID 3mzk

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