1urq

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of neuronal Q-SNAREs in complex with R-SNARE motif of Tomosyn

Structural highlights

1urq is a 4 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

STXB5_RAT Inhibits translocation of GLUT4 from intracellular vesicles to the plasma membrane (By similarity). Plays a regulatory role in calcium-dependent exocytosis and neurotransmitter release. Inhibits membrane fusion between transport vesicles and the plasma membrane. May modulate the assembly of trans-SNARE complexes between transport vesicles and the plasma membrane. Competes with STXBP1 for STX1 binding.^[1]

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 PubMed

Upon Ca2+ influx synaptic vesicles fuse with the plasma membrane and release their neurotransmitter cargo into the synaptic cleft. Key players during this process are the Q-SNAREs syntaxin 1a and SNAP-25 and the R-SNARE synaptobrevin 2. It is thought that these membrane proteins gradually assemble into a tight trans-SNARE complex between vesicular and plasma membrane, ultimately leading to membrane fusion. Tomosyn is a soluble protein of 130 kDa that contains a COOH-terminal R-SNARE motif but lacks a transmembrane anchor. Its R-SNARE motif forms a stable core SNARE complex with syntaxin 1a and SNAP-25. Here we present the crystal structure of this core tomosyn SNARE complex at 2.0-A resolution. It consists of a four-helical bundle very similar to that of the SNARE complex containing synaptobrevin. Most differences are found on the surface, where they prevented tight binding of complexin. Both complexes form with similar rates as assessed by CD spectroscopy. In addition, synaptobrevin cannot displace the tomosyn helix from the tight complex and vice versa, indicating that both SNARE complexes represent end products. Moreover, data bank searches revealed that the R-SNARE motif of tomosyn is highly conserved throughout all eukaryotic kingdoms. This suggests that the formation of a tight SNARE complex is important for the function of tomosyn.

Structural basis for the inhibitory role of tomosyn in exocytosis.,Pobbati AV, Razeto A, Boddener M, Becker S, Fasshauer D J Biol Chem. 2004 Nov 5;279(45):47192-200. Epub 2004 Aug 16. PMID:15316007^[2]

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

References

↑ Fujita Y, Shirataki H, Sakisaka T, Asakura T, Ohya T, Kotani H, Yokoyama S, Nishioka H, Matsuura Y, Mizoguchi A, Scheller RH, Takai Y. Tomosyn: a syntaxin-1-binding protein that forms a novel complex in the neurotransmitter release process. Neuron. 1998 May;20(5):905-15. PMID:9620695 doi:10.1016/s0896-6273(00)80472-9
↑ Pobbati AV, Razeto A, Boddener M, Becker S, Fasshauer D. Structural basis for the inhibitory role of tomosyn in exocytosis. J Biol Chem. 2004 Nov 5;279(45):47192-200. Epub 2004 Aug 16. PMID:15316007 doi:http://dx.doi.org/10.1074/jbc.M408767200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1urq"

@@ Line 1: / Line 1: @@
-==CRYSTAL STRUCTURE OF NEURONAL Q-SNARES IN COMPLEX WITH R-SNARE MOTIF OF TOMOSYN==
-<StructureSection load='1urq' size='340' side='right' caption='[[1urq]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+==Crystal structure of neuronal Q-SNAREs in complex with R-SNARE motif of Tomosyn==
+<StructureSection load='1urq' size='340' side='right'caption='[[1urq]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1urq]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1URQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1URQ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1urq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1URQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1URQ FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1br0|1br0]], [[1dn1|1dn1]], [[1ez3|1ez3]], [[1hvv|1hvv]], [[1jth|1jth]], [[1kil|1kil]], [[1n7s|1n7s]], [[1sfc|1sfc]], [[2bu0|2bu0]]</td></tr>
+</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&#8491;</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=1urq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1urq OCA], [http://pdbe.org/1urq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1urq RCSB], [http://www.ebi.ac.uk/pdbsum/1urq PDBsum]</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=1urq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1urq OCA], [https://pdbe.org/1urq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1urq RCSB], [https://www.ebi.ac.uk/pdbsum/1urq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1urq ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/SNP25_HUMAN SNP25_HUMAN]] t-SNARE involved in the molecular regulation of neurotransmitter release. May play an important role in the synaptic function of specific neuronal systems. Associates with proteins involved in vesicle docking and membrane fusion. Regulates plasma membrane recycling through its interaction with CENPF. [[http://www.uniprot.org/uniprot/STX1A_RAT STX1A_RAT]] Potentially involved in docking of synaptic vesicles at presynaptic active zones. May play a critical role in neurotransmitter exocytosis. May mediate Ca(2+)-regulation of exocytosis acrosomal reaction in sperm.
+[https://www.uniprot.org/uniprot/STXB5_RAT STXB5_RAT] Inhibits translocation of GLUT4 from intracellular vesicles to the plasma membrane (By similarity). Plays a regulatory role in calcium-dependent exocytosis and neurotransmitter release. Inhibits membrane fusion between transport vesicles and the plasma membrane. May modulate the assembly of trans-SNARE complexes between transport vesicles and the plasma membrane. Competes with STXBP1 for STX1 binding.<ref>PMID:9620695</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ur/1urq_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ur/1urq_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=1urq ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 29: / Line 30: @@
 ==See Also==
-*[[Flock house virus B2 protein Suppression of RNA Silencing|Flock house virus B2 protein Suppression of RNA Silencing]]
+*[[Flock house virus protein B2|Flock house virus protein B2]]
-*[[User:Wayne Decatur/Flock house virus B2 protein Suppression of RNA Silencing|User:Wayne Decatur/Flock house virus B2 protein Suppression of RNA Silencing]]
+*[[Synaptosomal-associated protein|Synaptosomal-associated protein]]
+*[[Syntaxin 3D structures|Syntaxin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Buffalo rat]]
+[[Category: Large Structures]]
-[[Category: Becker, S]]
+[[Category: Rattus norvegicus]]
-[[Category: Fasshauer, D]]
+[[Category: Becker S]]
-[[Category: Pobbati, A]]
+[[Category: Fasshauer D]]
-[[Category: Razeto, A]]
+[[Category: Pobbati A]]
-[[Category: Exocytosis]]
+[[Category: Razeto A]]
-[[Category: Four helical bundle]]
-[[Category: Tomosyn-snare complex]]
-[[Category: Transport protein]]

1urq

From Proteopedia

Current revision

Crystal structure of neuronal Q-SNAREs in complex with R-SNARE motif of Tomosyn

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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