3puk: Difference between revisions
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<StructureSection load='3puk' size='340' side='right'caption='[[3puk]], [[Resolution|resolution]] 3.05Å' scene=''> | <StructureSection load='3puk' size='340' side='right'caption='[[3puk]], [[Resolution|resolution]] 3.05Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3puk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3puk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2pjx 2pjx]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PUK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PUK 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]] 3.054Å</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=3puk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3puk OCA], [https://pdbe.org/3puk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3puk RCSB], [https://www.ebi.ac.uk/pdbsum/3puk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3puk 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=3puk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3puk OCA], [https://pdbe.org/3puk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3puk RCSB], [https://www.ebi.ac.uk/pdbsum/3puk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3puk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/STXB3_MOUSE STXB3_MOUSE] Together with STX4 and VAMP2, may play a role in insulin-dependent movement of GLUT4 and in docking/fusion of intracellular GLUT4-containing vesicles with the cell surface in adipocytes.<ref>PMID:9045631</ref> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mus musculus]] | ||
[[Category: Christie | [[Category: Christie MP]] | ||
[[Category: Collins | [[Category: Collins BM]] | ||
[[Category: Hu | [[Category: Hu S-H]] | ||
[[Category: Jarrott | [[Category: Jarrott R]] | ||
[[Category: Latham | [[Category: Latham CF]] | ||
[[Category: Lua | [[Category: Lua LHL]] | ||
[[Category: Martin | [[Category: Martin JL]] | ||
[[Category: Saez | [[Category: Saez NJ]] | ||
Latest revision as of 20:08, 1 November 2023
Re-refinement of the crystal structure of Munc18-3 and Syntaxin4 N-peptide complexRe-refinement of the crystal structure of Munc18-3 and Syntaxin4 N-peptide complex
Structural highlights
FunctionSTXB3_MOUSE Together with STX4 and VAMP2, may play a role in insulin-dependent movement of GLUT4 and in docking/fusion of intracellular GLUT4-containing vesicles with the cell surface in adipocytes.[1] Publication Abstract from PubMedMunc18-1 and Syntaxin1 are essential proteins for SNARE-mediated neurotransmission. Munc18-1 participates in synaptic vesicle fusion via dual roles: as a docking/chaperone protein by binding closed Syntaxin1, and as a fusion protein that binds SNARE complexes in a Syntaxin1 N-peptide dependent manner. The two roles are associated with a closed-open Syntaxin1 conformational transition. Here, we show that Syntaxin N-peptide binding to Munc18-1 is not highly selective, suggesting that other parts of the SNARE complex are involved in binding to Munc18-1. We also find that Syntaxin1, with an N peptide and a physically anchored C terminus, binds to Munc18-1 and that this complex can participate in SNARE complex formation. We report a Munc18-1-N-peptide crystal structure that, together with other data, reveals how Munc18-1 might transit from a conformation that binds closed Syntaxin1 to one that may be compatible with binding open Syntaxin1 and SNARE complexes. Our results suggest the possibility that structural transitions occur in both Munc18-1 and Syntaxin1 during their binary interaction. We hypothesize that Munc18-1 domain 3a undergoes a conformational change that may allow coiled-coil interactions with SNARE complexes. Possible roles for Munc18-1 domain 3a and Syntaxin1 N-peptide and C-terminal anchor in SNARE complex formation.,Hu SH, Christie MP, Saez NJ, Latham CF, Jarrott R, Lua LH, Collins BM, Martin JL Proc Natl Acad Sci U S A. 2010 Dec 30. PMID:21193638[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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