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3puk

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Revision as of 10:20, 4 August 2016

Re-refinement of the crystal structure of Munc18-3 and Syntaxin4 N-peptide complex

Structural highlights

3puk is a 4 chain structure with sequence from Lk3 transgenic mice. This structure supersedes the now removed PDB entry 2pjx. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2pjx, 3puj
Gene:	Stxbp3, Stxbp3a, Unc18c (LK3 transgenic mice)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] [STX4_MOUSE] Plasma membrane t-SNARE that mediates docking of transport vesicles. Necessary for the translocation of SLC2A4 from intracellular vesicles to the plasma membrane. Together with STXB3 and VAMP2, may also play a role in docking/fusion of intracellular GLUT4-containing vesicles with the cell surface in adipocytes and in docking of synaptic vesicles at presynaptic active zones.^[2] ^[3] ^[4]

Publication Abstract from PubMed

Munc18-1 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^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Tellam JT, Macaulay SL, McIntosh S, Hewish DR, Ward CW, James DE. Characterization of Munc-18c and syntaxin-4 in 3T3-L1 adipocytes. Putative role in insulin-dependent movement of GLUT-4. J Biol Chem. 1997 Mar 7;272(10):6179-86. PMID:9045631
↑ Tellam JT, Macaulay SL, McIntosh S, Hewish DR, Ward CW, James DE. Characterization of Munc-18c and syntaxin-4 in 3T3-L1 adipocytes. Putative role in insulin-dependent movement of GLUT-4. J Biol Chem. 1997 Mar 7;272(10):6179-86. PMID:9045631
↑ Min J, Okada S, Kanzaki M, Elmendorf JS, Coker KJ, Ceresa BP, Syu LJ, Noda Y, Saltiel AR, Pessin JE. Synip: a novel insulin-regulated syntaxin 4-binding protein mediating GLUT4 translocation in adipocytes. Mol Cell. 1999 Jun;3(6):751-60. PMID:10394363
↑ Pooley RD, Moynihan KL, Soukoulis V, Reddy S, Francis R, Lo C, Ma LJ, Bader DM. Murine CENPF interacts with syntaxin 4 in the regulation of vesicular transport. J Cell Sci. 2008 Oct 15;121(Pt 20):3413-21. doi: 10.1242/jcs.032847. Epub 2008, Sep 30. PMID:18827011 doi:10.1242/jcs.032847
↑ Hu SH, Christie MP, Saez NJ, Latham CF, Jarrott R, Lua LH, Collins BM, Martin JL. Possible roles for Munc18-1 domain 3a and Syntaxin1 N-peptide and C-terminal anchor in SNARE complex formation. Proc Natl Acad Sci U S A. 2010 Dec 30. PMID:21193638 doi:10.1073/pnas.0914906108

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3puk"

@@ Line 1: / Line 1: @@
 ==Re-refinement of the crystal structure of Munc18-3 and Syntaxin4 N-peptide complex==
 <StructureSection load='3puk' size='340' side='right' caption='[[3puk]], [[Resolution|resolution]] 3.05&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2pjx|2pjx]], [[3puj|3puj]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Stxbp3, Stxbp3a, Unc18c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3puk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3puk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3puk RCSB], [http://www.ebi.ac.uk/pdbsum/3puk PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3puk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3puk OCA], [http://pdbe.org/3puk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3puk RCSB], [http://www.ebi.ac.uk/pdbsum/3puk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3puk ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3puk" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

3puk

From Proteopedia

Revision as of 10:20, 4 August 2016

Re-refinement of the crystal structure of Munc18-3 and Syntaxin4 N-peptide complex

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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