1pd1
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1pd1]] is a 2 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=1PD1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PD1 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1pd1]] is a 2 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=1PD1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PD1 FirstGlance]. <br> | ||
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> |
| - | <tr id=' | + | <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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pd1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pd1 OCA], [https://pdbe.org/1pd1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pd1 RCSB], [https://www.ebi.ac.uk/pdbsum/1pd1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pd1 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=1pd1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pd1 OCA], [https://pdbe.org/1pd1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pd1 RCSB], [https://www.ebi.ac.uk/pdbsum/1pd1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pd1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/SEC24_YEAST SEC24_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. SEC24 specifically recruits cargo proteins like BET1 or SYS1 to the COPII vesicles. The SEC23/24 complex is also involved in internalisation of plasma membrane proteins like the maltose transporter.<ref>PMID:8548805</ref> <ref>PMID:9023343</ref> <ref>PMID:9428766</ref> <ref>PMID:10198022</ref> <ref>PMID:10753972</ref> <ref>PMID:10749860</ref> <ref>PMID:11086000</ref> <ref>PMID:10720463</ref> <ref>PMID:10712514</ref> <ref>PMID:12941277</ref> <ref>PMID:12655150</ref> <ref>PMID:14627716</ref> <ref>PMID:16269340</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=1pd1 ConSurf]. | </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=1pd1 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The COPII coat buds transport vesicles from the endoplasmic reticulum that incorporate cargo and SNARE molecules. Here, we show that recognition of the ER-Golgi SNAREs Bet1, Sed5, and Sec22 occurs through three binding sites on the Sec23/24 subcomplex of yeast COPII. The A site binds to the YNNSNPF motif of Sed5. The B site binds to Lxx-L/M-E sequences present in both the Bet1 and Sed5 molecules, as well as to the DxE cargo-sorting signal. A third, spatially distinct site binds to Sec22. COPII selects the free v-SNARE form of Bet1 because the LxxLE sequence is sequestered in the four-helix bundle of the v-/t-SNARE complex. COPII favors Sed5 within the Sed5/Bos1/Sec22 t-SNARE complex because t-SNARE assembly removes autoinhibitory contacts to expose the YNNSNPF motif. The COPII coat seems to be a specific conductor of the fusogenic forms of these SNAREs, suggesting how vesicle fusion specificity may be programmed during budding. | ||
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| - | SNARE selectivity of the COPII coat.,Mossessova E, Bickford LC, Goldberg J Cell. 2003 Aug 22;114(4):483-95. PMID:12941276<ref>PMID:12941276</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1pd1" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
| - | [[Category: Bickford | + | [[Category: Bickford LC]] |
| - | [[Category: Goldberg | + | [[Category: Goldberg J]] |
| - | [[Category: Mossessova | + | [[Category: Mossessova E]] |
| - | + | ||
Current revision
Crystal structure of the COPII coat subunit, Sec24, complexed with a peptide containing the DxE cargo sorting signal of yeast Sys1 protein
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