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| | ==Crystal Structure of the Sec13-Sec16 blade-inserted complex from Pichia pastoris== | | ==Crystal Structure of the Sec13-Sec16 blade-inserted complex from Pichia pastoris== |
| - | <StructureSection load='4l9o' size='340' side='right' caption='[[4l9o]], [[Resolution|resolution]] 1.60Å' scene=''> | + | <StructureSection load='4l9o' size='340' side='right'caption='[[4l9o]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4l9o]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Komagataella_pastoris_(strain_gs115_/_atcc_20864) Komagataella pastoris (strain gs115 / atcc 20864)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L9O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4L9O FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4l9o]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Komagataella_pastoris Komagataella pastoris] and [https://en.wikipedia.org/wiki/Komagataella_phaffii_GS115 Komagataella phaffii GS115]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L9O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4L9O FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SEC13, PP7435_Chr4-0919 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=644223 Komagataella pastoris (strain GS115 / ATCC 20864)])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> |
| - | <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=4l9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l9o OCA], [http://pdbe.org/4l9o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4l9o RCSB], [http://www.ebi.ac.uk/pdbsum/4l9o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4l9o ProSAT]</span></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=4l9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l9o OCA], [https://pdbe.org/4l9o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4l9o RCSB], [https://www.ebi.ac.uk/pdbsum/4l9o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4l9o ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SEC13_PICPG SEC13_PICPG]] 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. 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 (By similarity). | + | [https://www.uniprot.org/uniprot/Q45TY0_PICPA Q45TY0_PICPA] [https://www.uniprot.org/uniprot/SEC13_KOMPG SEC13_KOMPG] 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. 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 (By similarity).[UniProtKB:Q04491] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Hughson, F M]] | + | [[Category: Komagataella pastoris]] |
| - | [[Category: Jeffrey, P D]] | + | [[Category: Komagataella phaffii GS115]] |
| - | [[Category: McMahon, C]] | + | [[Category: Large Structures]] |
| - | [[Category: Ace1]] | + | [[Category: Hughson FM]] |
| - | [[Category: Beta propeller]] | + | [[Category: Jeffrey PD]] |
| - | [[Category: Cop-coated vesicle]] | + | [[Category: McMahon C]] |
| - | [[Category: Copii]]
| + | |
| - | [[Category: Endoplasmic reticulum]]
| + | |
| - | [[Category: Nuclear pore complex protein]]
| + | |
| - | [[Category: Protein transport]]
| + | |
| - | [[Category: Vesicle coat budding]]
| + | |
| Structural highlights
Function
Q45TY0_PICPA SEC13_KOMPG 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. 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 (By similarity).[UniProtKB:Q04491]
Publication Abstract from PubMed
During the budding of COPII vesicles from transitional ER (tER) sites, Sec16 has been proposed to play two distinct roles: negatively regulating COPII turnover, and organizing COPII assembly at tER sites. We tested these ideas using the yeast Pichia pastoris. Redistribution of Sec16 to the cytosol accelerates tER dynamics, supporting a negative regulatory role for Sec16. To evaluate a possible COPII organization role, we dissected the functional regions of Sec16. The central conserved domain (CCD), which had been implicated in coordinating COPII assembly, is actually dispensable for normal tER structure. An upstream conserved region (UCR) localizes Sec16 to tER sites. The UCR binds COPII components, and removal of COPII from tER sites also removes Sec16, indicating that COPII recruits Sec16 rather than the other way around. We propose that Sec16 does not in fact organize COPII. Instead, regulation of COPII turnover can account for the influence of Sec16 on tER sites.
Sec16 influences transitional ER sites by regulating rather than organizing COPII.,Bharucha N, Liu Y, Papanikou E, McMahon C, Esaki M, Jeffrey PD, Hughson FM, Glick BS Mol Biol Cell. 2013 Sep 4. PMID:24006484[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bharucha N, Liu Y, Papanikou E, McMahon C, Esaki M, Jeffrey PD, Hughson FM, Glick BS. Sec16 influences transitional ER sites by regulating rather than organizing COPII. Mol Biol Cell. 2013 Sep 4. PMID:24006484 doi:10.1091/mbc.E13-04-0185
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