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| | <StructureSection load='3efo' size='340' side='right'caption='[[3efo]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='3efo' size='340' side='right'caption='[[3efo]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3efo]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EFO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EFO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3efo]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EFO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EFO FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.7Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3eg9|3eg9]], [[3egd|3egd]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SEC23A ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), SEC24D ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3efo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3efo OCA], [https://pdbe.org/3efo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3efo RCSB], [https://www.ebi.ac.uk/pdbsum/3efo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3efo 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=3efo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3efo OCA], [https://pdbe.org/3efo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3efo RCSB], [https://www.ebi.ac.uk/pdbsum/3efo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3efo ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[https://www.uniprot.org/uniprot/SC23A_HUMAN SC23A_HUMAN]] Defects in SEC23A are the cause of craniolenticulosutural dysplasia (CLSD) [MIM:[https://omim.org/entry/607812 607812]]; also known as cranio-lenticulo-sutural dysplasia. CLSD is an autosomal recessive syndrome characterized by late-closing fontanels, sutural cataracts, facial dysmorphisms and skeletal defects.<ref>PMID:16980979</ref>
| + | [https://www.uniprot.org/uniprot/SC23A_HUMAN SC23A_HUMAN] Defects in SEC23A are the cause of craniolenticulosutural dysplasia (CLSD) [MIM:[https://omim.org/entry/607812 607812]; also known as cranio-lenticulo-sutural dysplasia. CLSD is an autosomal recessive syndrome characterized by late-closing fontanels, sutural cataracts, facial dysmorphisms and skeletal defects.<ref>PMID:16980979</ref> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/SC23A_HUMAN SC23A_HUMAN]] Component of the COPII coat, that covers ER-derived vesicles involved in transport from the endoplasmic reticulum to the Golgi apparatus. COPII acts in the cytoplasm to promote the transport of secretory, plasma membrane, and vacuolar proteins from the endoplasmic reticulum to the Golgi complex. [[https://www.uniprot.org/uniprot/SC24D_HUMAN SC24D_HUMAN]] Component of the COPII coat, that covers ER-derived vesicles involved in transport from the endoplasmic reticulum to the Golgi apparatus. COPII acts in the cytoplasm to promote the transport of secretory, plasma membrane, and vacuolar proteins from the endoplasmic reticulum to the Golgi complex.
| + | [https://www.uniprot.org/uniprot/SC23A_HUMAN SC23A_HUMAN] Component of the COPII coat, that covers ER-derived vesicles involved in transport from the endoplasmic reticulum to the Golgi apparatus. COPII acts in the cytoplasm to promote the transport of secretory, plasma membrane, and vacuolar proteins from the endoplasmic reticulum to the Golgi complex. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ef/3efo_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ef/3efo_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Goldberg, J]] | + | [[Category: Goldberg J]] |
| - | [[Category: Mancias, J D]] | + | [[Category: Mancias JD]] |
| - | [[Category: Coat protein]]
| + | |
| - | [[Category: Copii]]
| + | |
| - | [[Category: Disease mutation]]
| + | |
| - | [[Category: Endoplasmic reticulum]]
| + | |
| - | [[Category: Er-golgi transport]]
| + | |
| - | [[Category: Golgi apparatus]]
| + | |
| - | [[Category: Membrane]]
| + | |
| - | [[Category: Protein transport]]
| + | |
| - | [[Category: Transport]]
| + | |
| - | [[Category: Transport signal]]
| + | |
| Structural highlights
Disease
SC23A_HUMAN Defects in SEC23A are the cause of craniolenticulosutural dysplasia (CLSD) [MIM:607812; also known as cranio-lenticulo-sutural dysplasia. CLSD is an autosomal recessive syndrome characterized by late-closing fontanels, sutural cataracts, facial dysmorphisms and skeletal defects.[1]
Function
SC23A_HUMAN Component of the COPII coat, that covers ER-derived vesicles involved in transport from the endoplasmic reticulum to the Golgi apparatus. COPII acts in the cytoplasm to promote the transport of secretory, plasma membrane, and vacuolar proteins from the endoplasmic reticulum to the Golgi complex.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Genomic analysis shows that the increased complexity of trafficking pathways in mammalian cells involves an expansion of the number of SNARE, Rab and COP proteins. Thus, the human genome encodes four forms of Sec24, the cargo selection subunit of the COPII vesicular coat, and this is proposed to increase the range of cargo accommodated by human COPII-coated vesicles. In this study, we combined X-ray crystallographic and biochemical analysis with functional assays of cargo packaging into COPII vesicles to establish molecular mechanisms for cargo discrimination by human Sec24 subunits. A conserved IxM packaging signal binds in a surface groove of Sec24c and Sec24d, but the groove is occluded in the Sec24a and Sec24b subunits. Conversely, LxxLE class transport signals and the DxE signal of VSV glycoprotein are selectively bound by Sec24a and Sec24b subunits. A comparative analysis of crystal structures of the four human Sec24 isoforms establishes the structural determinants for discrimination among these transport signals, and provides a framework to understand how an expansion of coat subunits extends the range of cargo proteins packaged into COPII-coated vesicles.
Structural basis of cargo membrane protein discrimination by the human COPII coat machinery.,Mancias JD, Goldberg J EMBO J. 2008 Nov 5;27(21):2918-28. Epub 2008 Oct 9. PMID:18843296[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Boyadjiev SA, Fromme JC, Ben J, Chong SS, Nauta C, Hur DJ, Zhang G, Hamamoto S, Schekman R, Ravazzola M, Orci L, Eyaid W. Cranio-lenticulo-sutural dysplasia is caused by a SEC23A mutation leading to abnormal endoplasmic-reticulum-to-Golgi trafficking. Nat Genet. 2006 Oct;38(10):1192-7. Epub 2006 Sep 17. PMID:16980979 doi:10.1038/ng1876
- ↑ Mancias JD, Goldberg J. Structural basis of cargo membrane protein discrimination by the human COPII coat machinery. EMBO J. 2008 Nov 5;27(21):2918-28. Epub 2008 Oct 9. PMID:18843296 doi:http://dx.doi.org/10.1038/emboj.2008.208
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