1qqe
From Proteopedia
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==CRYSTAL STRUCTURE OF THE VESICULAR TRANSPORT PROTEIN SEC17== | ==CRYSTAL STRUCTURE OF THE VESICULAR TRANSPORT PROTEIN SEC17== | ||
| - | <StructureSection load='1qqe' size='340' side='right' caption='[[1qqe]], [[Resolution|resolution]] 2.90Å' scene=''> | + | <StructureSection load='1qqe' size='340' side='right'caption='[[1qqe]], [[Resolution|resolution]] 2.90Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1qqe]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1qqe]] is a 1 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=1QQE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QQE FirstGlance]. <br> |
| - | </td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> |
| - | <table> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qqe OCA], [https://pdbe.org/1qqe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qqe RCSB], [https://www.ebi.ac.uk/pdbsum/1qqe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qqe ProSAT]</span></td></tr> |
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/SEC17_YEAST SEC17_YEAST] SNARE complex protein that binds to cis-SNARE complexes on membranes and is required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus and for homotypic vacuole fusion. During the priming step of membrane fusion, is released from cis-SNARE complexes by SEC18 to establish a pool of unpaired SNAREs, which are required for interactions in trans during docking and fusion steps. Can displace HOPS from SNARE complexes, which may be a prerequisite for trans-SNARE complex disassembly and subsequent rounds of priming, docking and fusion.<ref>PMID:8620540</ref> <ref>PMID:8670830</ref> <ref>PMID:9144293</ref> <ref>PMID:15889152</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qq/1qqe_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qq/1qqe_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| - | </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/ | + | </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=1qqe ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | SNAP proteins play an essential role in membrane trafficking in eukaryotic cells. They activate and recycle SNARE proteins by serving as adaptors between SNAREs and the cytosolic chaperone NSF. We have determined the crystal structure of Sec17, the yeast homolog of alpha-SNAP, to 2.9 A resolution. Sec17 is composed of an N-terminal twisted sheet of alpha-helical hairpins and a C-terminal alpha-helical bundle. The N-terminal sheet has local similarity to the tetratricopeptide repeats from protein phosphatase 5 but has a different overall twist. Sec17 also shares structural features with HEAT and clathrin heavy chain repeats. Possible models of SNAP:SNARE binding suggest that SNAPs may function as lever arms, transmitting forces generated by conformational changes in NSF/Sec18 to drive disassembly of SNARE complexes. | ||
| - | |||
| - | Crystal structure of the vesicular transport protein Sec17: implications for SNAP function in SNARE complex disassembly.,Rice LM, Brunger AT Mol Cell. 1999 Jul;4(1):85-95. PMID:10445030<ref>PMID:10445030</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
| - | [[Category: Brunger | + | [[Category: Brunger AT]] |
| - | [[Category: Rice | + | [[Category: Rice LM]] |
| - | + | ||
| - | + | ||
Current revision
CRYSTAL STRUCTURE OF THE VESICULAR TRANSPORT PROTEIN SEC17
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