1f82: Difference between revisions

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[[Image:1f82.jpg|left|200px]]<br /><applet load="1f82" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1f82.jpg|left|200px]]
caption="1f82, resolution 2.20&Aring;" />
 
'''BOTULINUM NEUROTOXIN TYPE B CATALYTIC DOMAIN'''<br />
{{Structure
|PDB= 1f82 |SIZE=350|CAPTION= <scene name='initialview01'>1f82</scene>, resolution 2.20&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Bontoxilysin Bontoxilysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.69 3.4.24.69]
|GENE=
}}
 
'''BOTULINUM NEUROTOXIN TYPE B CATALYTIC DOMAIN'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1F82 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_botulinum Clostridium botulinum] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Bontoxilysin Bontoxilysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.69 3.4.24.69] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F82 OCA].  
1F82 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_botulinum Clostridium botulinum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F82 OCA].  


==Reference==
==Reference==
Cocrystal structure of synaptobrevin-II bound to botulinum neurotoxin type B at 2.0 A resolution., Hanson MA, Stevens RC, Nat Struct Biol. 2000 Aug;7(8):687-92. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10932255 10932255]
Cocrystal structure of synaptobrevin-II bound to botulinum neurotoxin type B at 2.0 A resolution., Hanson MA, Stevens RC, Nat Struct Biol. 2000 Aug;7(8):687-92. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10932255 10932255]
[[Category: Bontoxilysin]]
[[Category: Bontoxilysin]]
[[Category: Clostridium botulinum]]
[[Category: Clostridium botulinum]]
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[[Category: zinc dependent protease]]
[[Category: zinc dependent protease]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:35:53 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:05:45 2008''

Revision as of 12:05, 20 March 2008

File:1f82.jpg


PDB ID 1f82

Drag the structure with the mouse to rotate
, resolution 2.20Å
Ligands:
Activity: Bontoxilysin, with EC number 3.4.24.69
Coordinates: save as pdb, mmCIF, xml



BOTULINUM NEUROTOXIN TYPE B CATALYTIC DOMAIN


OverviewOverview

Botulinum neurotoxin serotype B is a zinc protease that disrupts neurotransmitter release by cleaving synaptobrevin-II (Sb2), one of three SNARE proteins involved in neuronal synaptic vesicle fusion. The three-dimensional crystal structure of the apo botulinum neurotoxin serotype B catalytic domain (BoNT/B-LC) has been determined to 2.2 A resolution, and the complex of cleaved Sb2 with the catalytic domain (Sb2-BoNT/B-LC) has been determined to 2.0 A resolution. A comparison of the holotoxin catalytic domain and the isolated BoNT/B-LC structure shows a rearrangement of three active site loops. This rearrangement exposes the BoNT/B active site. The Sb2-BoNT/B-LC structure illustrates two distinct binding regions, which explains the specificity of each botulinum neurotoxin for its synaptic vesicle protein. This observation provides an explanation for the proposed cooperativity between binding of full-length substrate and catalysis and suggest a mechanism of synaptobrevin proteolysis employed by the clostridial neurotoxins.

About this StructureAbout this Structure

1F82 is a Single protein structure of sequence from Clostridium botulinum. Full crystallographic information is available from OCA.

ReferenceReference

Cocrystal structure of synaptobrevin-II bound to botulinum neurotoxin type B at 2.0 A resolution., Hanson MA, Stevens RC, Nat Struct Biol. 2000 Aug;7(8):687-92. PMID:10932255

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