1f82
From Proteopedia
(New page: 200px<br /><applet load="1f82" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f82, resolution 2.20Å" /> '''BOTULINUM NEUROTOXIN...) |
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| - | [[Image:1f82.jpg|left|200px]]<br /><applet load="1f82" size=" | + | [[Image:1f82.jpg|left|200px]]<br /><applet load="1f82" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1f82, resolution 2.20Å" /> | caption="1f82, resolution 2.20Å" /> | ||
'''BOTULINUM NEUROTOXIN TYPE B CATALYTIC DOMAIN'''<br /> | '''BOTULINUM NEUROTOXIN TYPE B CATALYTIC DOMAIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Botulinum neurotoxin serotype B is a zinc protease that disrupts | + | 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 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 ZN 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:// | + | 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]. |
==Reference== | ==Reference== | ||
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[[Category: Clostridium botulinum]] | [[Category: Clostridium botulinum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Hanson, M | + | [[Category: Hanson, M A.]] |
| - | [[Category: Stevens, R | + | [[Category: Stevens, R C.]] |
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: botulinum neurotoxin]] | [[Category: botulinum neurotoxin]] | ||
[[Category: zinc dependent protease]] | [[Category: zinc dependent protease]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:35:53 2008'' |
Revision as of 10:35, 21 February 2008
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BOTULINUM NEUROTOXIN TYPE B CATALYTIC DOMAIN
Overview
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 Structure
1F82 is a Single protein structure of sequence from Clostridium botulinum with as ligand. Active as Bontoxilysin, with EC number 3.4.24.69 Full crystallographic information is available from OCA.
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:10932255
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