3ipd: Difference between revisions
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<StructureSection load='3ipd' size='340' side='right'caption='[[3ipd]], [[Resolution|resolution]] 4.80Å' scene=''> | <StructureSection load='3ipd' size='340' side='right'caption='[[3ipd]], [[Resolution|resolution]] 4.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3ipd]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3ipd]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3hd9 3hd9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IPD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IPD 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]] 4.8Å</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=3ipd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ipd OCA], [https://pdbe.org/3ipd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ipd RCSB], [https://www.ebi.ac.uk/pdbsum/3ipd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ipd 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=3ipd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ipd OCA], [https://pdbe.org/3ipd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ipd RCSB], [https://www.ebi.ac.uk/pdbsum/3ipd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ipd ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/VAMP2_RAT VAMP2_RAT] Involved in the targeting and/or fusion of transport vesicles to their target membrane (By similarity). | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Jahn | [[Category: Rattus norvegicus]] | ||
[[Category: Stein | [[Category: Jahn R]] | ||
[[Category: Wahl | [[Category: Stein A]] | ||
[[Category: Weber | [[Category: Wahl MC]] | ||
[[Category: Weber G]] | |||
Latest revision as of 19:01, 1 November 2023
Helical extension of the neuronal SNARE complex into the membrane, spacegroup I 21 21 21Helical extension of the neuronal SNARE complex into the membrane, spacegroup I 21 21 21
Structural highlights
FunctionVAMP2_RAT Involved in the targeting and/or fusion of transport vesicles to their target membrane (By similarity). 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 PubMedNeurotransmission relies on synaptic vesicles fusing with the membrane of nerve cells to release their neurotransmitter content into the synaptic cleft, a process requiring the assembly of several members of the SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) family. SNAREs represent an evolutionarily conserved protein family that mediates membrane fusion in the secretory and endocytic pathways of eukaryotic cells. On membrane contact, these proteins assemble in trans between the membranes as a bundle of four alpha-helices, with the energy released during assembly being thought to drive fusion. However, it is unclear how the energy is transferred to the membranes and whether assembly is conformationally linked to fusion. Here, we report the X-ray structure of the neuronal SNARE complex, consisting of rat syntaxin 1A, SNAP-25 and synaptobrevin 2, with the carboxy-terminal linkers and transmembrane regions at 3.4 A resolution. The structure shows that assembly proceeds beyond the already known core SNARE complex, resulting in a continuous helical bundle that is further stabilized by side-chain interactions in the linker region. Our results suggest that the final phase of SNARE assembly is directly coupled to membrane merger. Helical extension of the neuronal SNARE complex into the membrane.,Stein A, Weber G, Wahl MC, Jahn R Nature. 2009 Jul 23;460(7254):525-8. Epub 2009 Jul 1. PMID:19571812[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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