1s94

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of the Habc domain of neuronal syntaxin from the squid Loligo pealei

Structural highlights

1s94 is a 2 chain structure with sequence from Doryteuthis pealeii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.34Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

O46345_DORPE

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

BACKGROUND: Intracellular membrane fusion processes are mediated by the spatial and temporal control of SNARE complex assembly that results in the formation of a four-helical bundle, composed of one vesicle SNARE and three target membrane SNARE polypeptide chains. Syntaxins are essential t-SNAREs and are characterized by an N-terminal Habc domain, a flexible linker region, a coiled-coil or SNARE motif and a membrane anchor. The N-terminal Habc domain fulfills important regulatory functions while the coiled-coil motif, present in all SNAREs, is sufficient for SNARE complex formation, which is thought to drive membrane fusion. RESULTS: Here we report the crystal structure of the Habc domain of neuronal syntaxin from the squid Loligo pealei, s-syntaxin. Squid Habc crystallizes as a dimer and the monomer structure consists of a three-helical bundle. One molecule is strikingly similar to mammalian syntaxin 1A while the second one shows a structural deviation from the common fold in that the C-terminal part of helix C unwinds and adopts an extended conformation. CONCLUSION: Conservation of surface residues indicates that the cytosolic part of s-syntaxin can adopt an auto-inhibitory closed conformation that may bind squid neuronal Sec1, s-Sec1, in the same manner as observed in structure of the rat nSec1/syntaxin 1A complex. Furthermore, despite the overall structural similarity, the observed changes at the C-terminus of one molecule indicate structural plasticity in neuronal syntaxin. Implications of the structural conservation and the changes are discussed with respect to potential Habc domain binding partners such as Munc13, which facilitates the transition from the closed to the open conformation.

Crystal structure of the Habc domain of neuronal syntaxin from the squid Loligo pealei reveals conformational plasticity at its C-terminus.,Bracher A, Weissenhorn W BMC Struct Biol. 2004 Mar 15;4:6. PMID:15113421^[1]

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

References

↑ Bracher A, Weissenhorn W. Crystal structure of the Habc domain of neuronal syntaxin from the squid Loligo pealei reveals conformational plasticity at its C-terminus. BMC Struct Biol. 2004 Mar 15;4:6. PMID:15113421 doi:10.1186/1472-6807-4-6

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/1s94"

Categories: Doryteuthis pealeii | Large Structures | Bracher A | Weissenhorn W

@@ Line 3: / Line 3: @@
 <StructureSection load='1s94' size='340' side='right'caption='[[1s94]], [[Resolution|resolution]] 3.34&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1s94]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S94 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S94 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1s94]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Doryteuthis_pealeii Doryteuthis pealeii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S94 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S94 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1epu|1epu]], [[1l4a|1l4a]], [[1br0|1br0]], [[1dn1|1dn1]], [[1ez3|1ez3]]</div></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]] 3.34&#8491;</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=1s94 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s94 OCA], [https://pdbe.org/1s94 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s94 RCSB], [https://www.ebi.ac.uk/pdbsum/1s94 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s94 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/O46345_DORPE O46345_DORPE]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 12: / Line 14: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/s9/1s94_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 33: / Line 35: @@
 __TOC__
 </StructureSection>
+[[Category: Doryteuthis pealeii]]
 [[Category: Large Structures]]
-[[Category: Bracher, A]]
+[[Category: Bracher A]]
-[[Category: Weissenhorn, W]]
+[[Category: Weissenhorn W]]
-[[Category: Endocytosis-exocytosis complex]]
-[[Category: Structural plasticity]]
-[[Category: Three helix bundle]]

1s94

From Proteopedia

Current revision

Crystal structure of the Habc domain of neuronal syntaxin from the squid Loligo pealei

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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