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1xtg

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Revision as of 10:19, 6 January 2021

Crystal structure of NEUROTOXIN BONT/A complexed with Synaptosomal-associated protein 25

Structural highlights

1xtg is a 2 chain structure with sequence from "bacillus_botulinus"_van_ermengem_1896 "bacillus botulinus" van ermengem 1896 and Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1xtf
Gene:	SNAP25, SNAP (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.

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

Clostridal neurotoxins (CNTs) are the causative agents of the neuroparalytic diseases botulism and tetanus. CNTs impair neuronal exocytosis through specific proteolysis of essential proteins called SNAREs. SNARE assembly into a low-energy ternary complex is believed to catalyse membrane fusion, precipitating neurotransmitter release; this process is attenuated in response to SNARE proteolysis. Site-specific SNARE hydrolysis is catalysed by the CNT light chains, a unique group of zinc-dependent endopeptidases. The means by which a CNT properly identifies and cleaves its target SNARE has been a subject of much speculation; it is thought to use one or more regions of enzyme-substrate interaction remote from the active site (exosites). Here we report the first structure of a CNT endopeptidase in complex with its target SNARE at a resolution of 2.1 A: botulinum neurotoxin serotype A (BoNT/A) protease bound to human SNAP-25. The structure, together with enzyme kinetic data, reveals an array of exosites that determine substrate specificity. Substrate orientation is similar to that of the general zinc-dependent metalloprotease thermolysin. We observe significant structural changes near the toxin's catalytic pocket upon substrate binding, probably serving to render the protease competent for catalysis. The novel structures of the substrate-recognition exosites could be used for designing inhibitors specific to BoNT/A.

Substrate recognition strategy for botulinum neurotoxin serotype A.,Breidenbach MA, Brunger AT Nature. 2004 Dec 16;432(7019):925-9. Epub 2004 Dec 12. PMID:15592454^[1]

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

References

↑ Breidenbach MA, Brunger AT. Substrate recognition strategy for botulinum neurotoxin serotype A. Nature. 2004 Dec 16;432(7019):925-9. Epub 2004 Dec 12. PMID:15592454 doi:http://dx.doi.org/10.1038/nature03123

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/1xtg"

@@ Line 1: / Line 1: @@
 ==Crystal structure of NEUROTOXIN BONT/A complexed with Synaptosomal-associated protein 25==
-<StructureSection load='1xtg' size='340' side='right' caption='[[1xtg]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
+<StructureSection load='1xtg' size='340' side='right'caption='[[1xtg]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1xtg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_botulinus"_van_ermengem_1896 "bacillus botulinus" van ermengem 1896] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XTG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XTG FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1xtg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_botulinus"_van_ermengem_1896 "bacillus botulinus" van ermengem 1896] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XTG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1XTG FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1xtf|1xtf]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1xtf|1xtf]]</div></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SNAP25, SNAP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=1xtg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xtg OCA], [http://pdbe.org/1xtg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xtg RCSB], [http://www.ebi.ac.uk/pdbsum/1xtg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xtg ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1xtg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xtg OCA], [http://pdbe.org/1xtg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xtg RCSB], [http://www.ebi.ac.uk/pdbsum/1xtg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xtg ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 32: / Line 32: @@
 ==See Also==
-*[[Botulinum neurotoxin|Botulinum neurotoxin]]
+*[[Botulinum neurotoxin 3D structures|Botulinum neurotoxin 3D structures]]
+*[[Synaptosomal-associated protein|Synaptosomal-associated protein]]
 == References ==
 <references/>
@@ Line 39: / Line 40: @@
 [[Category: Bacillus botulinus van ermengem 1896]]
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Breidenbach, M A]]
 [[Category: Brunger, A T]]

1xtg

From Proteopedia

Revision as of 10:19, 6 January 2021

Crystal structure of NEUROTOXIN BONT/A complexed with Synaptosomal-associated protein 25

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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