6f0o: Difference between revisions
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<StructureSection load='6f0o' size='340' side='right' caption='[[6f0o]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='6f0o' size='340' side='right' caption='[[6f0o]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6f0o]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F0O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6F0O FirstGlance]. <br> | <table><tr><td colspan='2'>[[6f0o]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Clobm Clobm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F0O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6F0O FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PPI:PROPANOIC+ACID'>PPI</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PPI:PROPANOIC+ACID'>PPI</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">botA, CLK_A0076 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=498214 CLOBM])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></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=6f0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f0o OCA], [http://pdbe.org/6f0o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f0o RCSB], [http://www.ebi.ac.uk/pdbsum/6f0o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f0o ProSAT]</span></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=6f0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f0o OCA], [http://pdbe.org/6f0o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f0o RCSB], [http://www.ebi.ac.uk/pdbsum/6f0o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f0o ProSAT]</span></td></tr> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Bontoxilysin]] | [[Category: Bontoxilysin]] | ||
[[Category: Clobm]] | |||
[[Category: Acharya, K R]] | [[Category: Acharya, K R]] | ||
[[Category: Davies, J R]] | [[Category: Davies, J R]] | ||
Latest revision as of 09:57, 4 April 2018
Botulinum neurotoxin A3 Hc domainBotulinum neurotoxin A3 Hc domain
Structural highlights
Publication Abstract from PubMedClostridium botulinum neurotoxins (BoNTs) cause the life-threatening condition, botulism. However, while they have the potential to cause serious harm, they are increasingly being utilised for therapeutic applications. BoNTs comprise of seven distinct serotypes termed BoNT/A through BoNT/G, with the most widely characterised being sub-serotype BoNT/A1. Each BoNT consists of three structurally distinct domains, a binding domain (HC), a translocation domain (HN), and a proteolytic domain (LC). The HC domain is responsible for the highly specific targeting of the neurotoxin to neuronal cell membranes. Here, we present two high-resolution structures of the binding domain of subtype BoNT/A3 (HC/A3) and BoNT/A4 (HC/A4) at 1.6A and 1.34A resolution, respectively. The structures of both proteins share a high degree of similarity to other known BoNT HC domains whilst containing some subtle differences, and are of benefit to research into therapeutic neurotoxins with novel characteristics. High resolution crystal structures of Clostridium botulinum neurotoxin A3 and A4 binding domains.,Davies JR, Rees J, Liu SM, Acharya KR J Struct Biol. 2017 Dec 26. pii: S1047-8477(17)30233-2. doi:, 10.1016/j.jsb.2017.12.010. PMID:29288126[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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