2pm7

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{{Seed}}
 
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[[Image:2pm7.png|left|200px]]
 
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==Crystal structure of yeast Sec13/31 edge element of the COPII vesicular coat, selenomethionine version==
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The line below this paragraph, containing "STRUCTURE_2pm7", creates the "Structure Box" on the page.
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<StructureSection load='2pm7' size='340' side='right'caption='[[2pm7]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2pm7]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PM7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PM7 FirstGlance]. <br>
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2pm6|2pm6]], [[2pm9|2pm9]]</div></td></tr>
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{{STRUCTURE_2pm7| PDB=2pm7 | SCENE= }}
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">WEB1, SEC31 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), SEC13, ANU3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=2pm7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pm7 OCA], [https://pdbe.org/2pm7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pm7 RCSB], [https://www.ebi.ac.uk/pdbsum/2pm7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pm7 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[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> [[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/pm/2pm7_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=2pm7 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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COPII-coated vesicles export newly synthesized proteins from the endoplasmic reticulum. The COPII coat consists of the Sec23/24-Sar1 complex that selects cargo and the Sec13/31 assembly unit that can polymerize into an octahedral cage and deform the membrane into a bud. Crystallographic analysis of the assembly unit reveals a 28 nm long rod comprising a central alpha-solenoid dimer capped by two beta-propeller domains at each end. We construct a molecular model of the COPII cage by fitting Sec13/31 crystal structures into a recently determined electron microscopy density map. The vertex geometry involves four copies of the Sec31 beta-propeller that converge through their axial ends; there is no interdigitation of assembly units of the kind seen in clathrin cages. We also propose that the assembly unit has a central hinge-an arrangement of interlocked alpha-solenoids-about which it can bend to adapt to cages of variable curvature.
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===Crystal structure of yeast Sec13/31 edge element of the COPII vesicular coat, selenomethionine version===
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Structure and organization of coat proteins in the COPII cage.,Fath S, Mancias JD, Bi X, Goldberg J Cell. 2007 Jun 29;129(7):1325-36. PMID:17604721<ref>PMID:17604721</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2pm7" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 17604721 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17604721}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Atcc 18824]]
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2PM7 is a 4 chains structure of sequences 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=2PM7 OCA].
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[[Category: Large Structures]]
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[[Category: Bi, X]]
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==Reference==
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[[Category: Fath, S]]
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<ref group="xtra">PMID:17604721</ref><references group="xtra"/>
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[[Category: Goldberg, J]]
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Mancias, J D]]
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[[Category: Bi, X.]]
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[[Category: Fath, S.]]
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[[Category: Goldberg, J.]]
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[[Category: Mancias, J D.]]
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[[Category: Alpha solenoid]]
[[Category: Alpha solenoid]]
[[Category: Beta propeller]]
[[Category: Beta propeller]]
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[[Category: Protein transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 12:58:41 2009''
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Current revision

Crystal structure of yeast Sec13/31 edge element of the COPII vesicular coat, selenomethionine version

PDB ID 2pm7

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