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1cr5

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(New page: 200px<br /><applet load="1cr5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cr5, resolution 2.3&Aring;" /> '''N-TERMINAL DOMAIN OF ...)
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[[Image:1cr5.jpg|left|200px]]<br /><applet load="1cr5" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1cr5, resolution 2.3&Aring;" />
 
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'''N-TERMINAL DOMAIN OF SEC18P'''<br />
 
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==Overview==
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==N-TERMINAL DOMAIN OF SEC18P==
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Yeast Sec18p and its mammalian orthologue N-ethylmaleimide-sensitive, fusion protein (NSF) are hexameric ATPases with a central role in vesicle, trafficking. Aided by soluble adapter factors (SNAPs), Sec18p/NSF induces, ATP-dependent disassembly of a complex of integral membrane proteins from, the vesicle and target membranes (SNAP receptors). During the ATP, hydrolysis cycle, the Sec18p/NSF homohexamer undergoes a large-scale, conformational change involving repositioning of the most N terminal of, the three domains of each protomer, a domain that is required for, SNAP-mediated interaction with SNAP receptors. Whether an internal, conformational change in the N-terminal domains accompanies their, reorientation with respect to the rest of the hexamer remains to be, addressed. We have determined the structure of the N-terminal domain from, Sec18p by x-ray crystallography. The Sec18p N-terminal domain consists of, two beta-sheet-rich subdomains connected by a short linker. A conserved, basic cleft opposite the linker may constitute a SNAP-binding site., Despite structural variability in the linker region and in an adjacent, loop, all three independent molecules in the crystal asymmetric unit have, the identical subdomain interface, supporting the notion that this, interface is a preferred packing arrangement. However, the linker, flexibility allows for the possibility that other subdomain orientations, may be sampled.
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<StructureSection load='1cr5' size='340' side='right'caption='[[1cr5]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1cr5]] is a 3 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=1CR5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CR5 FirstGlance]. <br>
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1CR5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with NEN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CR5 OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NEN:1-ETHYL-PYRROLIDINE-2,5-DIONE'>NEN</scene></td></tr>
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==Reference==
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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=1cr5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cr5 OCA], [https://pdbe.org/1cr5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cr5 RCSB], [https://www.ebi.ac.uk/pdbsum/1cr5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cr5 ProSAT]</span></td></tr>
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Crystal structure of the Sec18p N-terminal domain., Babor SM, Fass D, Proc Natl Acad Sci U S A. 1999 Dec 21;96(26):14759-64. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10611286 10611286]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SEC18_YEAST SEC18_YEAST] Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seems to function as a fusion protein required for the delivery of cargo proteins to all compartments of the Golgi stack independent of vesicle origin.
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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/cr/1cr5_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=1cr5 ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Babor SM]]
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[[Category: Babor, S.M.]]
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[[Category: Fass D]]
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[[Category: Fass, D.]]
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[[Category: NEN]]
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[[Category: double-psi beta barrel]]
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[[Category: vesicle fusion]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:41:40 2007''
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Current revision

N-TERMINAL DOMAIN OF SEC18P

PDB ID 1cr5

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