1f82: Difference between revisions
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==BOTULINUM NEUROTOXIN TYPE B CATALYTIC DOMAIN== | ==BOTULINUM NEUROTOXIN TYPE B CATALYTIC DOMAIN== | ||
<StructureSection load='1f82' size='340' side='right' caption='[[1f82]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='1f82' size='340' side='right'caption='[[1f82]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1f82]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_botulinus"_van_ermengem_1896 "bacillus botulinus" van ermengem 1896]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F82 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F82 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1f82]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_botulinus"_van_ermengem_1896 "bacillus botulinus" van ermengem 1896]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F82 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F82 FirstGlance]. <br> | ||
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==See Also== | ==See Also== | ||
*[[Botulinum neurotoxin|Botulinum neurotoxin]] | *[[Botulinum neurotoxin 3D structures|Botulinum neurotoxin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Bacillus botulinus van ermengem 1896]] | [[Category: Bacillus botulinus van ermengem 1896]] | ||
[[Category: Bontoxilysin]] | [[Category: Bontoxilysin]] | ||
[[Category: Large Structures]] | |||
[[Category: Hanson, M A]] | [[Category: Hanson, M A]] | ||
[[Category: Stevens, R C]] | [[Category: Stevens, R C]] | ||
Revision as of 11:46, 16 October 2019
BOTULINUM NEUROTOXIN TYPE B CATALYTIC DOMAINBOTULINUM NEUROTOXIN TYPE B CATALYTIC DOMAIN
Structural highlights
Function[BXB_CLOBO] Botulinum toxin acts by inhibiting neurotransmitter release. It binds to peripheral neuronal synapses, is internalized and moves by retrograde transport up the axon into the spinal cord where it can move between postsynaptic and presynaptic neurons. It inhibits neurotransmitter release by acting as a zinc endopeptidase that cleaves the '76-Gln-|-Phe-77' bond of synaptobrevin-2. 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 PubMedBotulinum 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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