3v0c: Difference between revisions
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==4.3 angstrom crystal structure of an inactive BoNT/A (E224Q/R363A/Y366F)== | ==4.3 angstrom crystal structure of an inactive BoNT/A (E224Q/R363A/Y366F)== | ||
<StructureSection load='3v0c' size='340' side='right' caption='[[3v0c]], [[Resolution|resolution]] 4.30Å' scene=''> | <StructureSection load='3v0c' size='340' side='right'caption='[[3v0c]], [[Resolution|resolution]] 4.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3v0c]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3v0c]] is a 1 chain structure with sequence from [https://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=3V0C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V0C FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bont/a, boNT/A, bonta ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bont/a, boNT/A, bonta ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1491 "Bacillus botulinus" van Ermengem 1896])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3v0c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v0c OCA], [https://pdbe.org/3v0c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v0c RCSB], [https://www.ebi.ac.uk/pdbsum/3v0c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v0c ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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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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</StructureSection> | </StructureSection> | ||
[[Category: Bacillus botulinus van ermengem 1896]] | [[Category: Bacillus botulinus van ermengem 1896]] | ||
[[Category: Large Structures]] | |||
[[Category: Bigalke, H]] | [[Category: Bigalke, H]] | ||
[[Category: Gu, S]] | [[Category: Gu, S]] | ||
Revision as of 11:20, 20 July 2022
4.3 angstrom crystal structure of an inactive BoNT/A (E224Q/R363A/Y366F)4.3 angstrom crystal structure of an inactive BoNT/A (E224Q/R363A/Y366F)
Structural highlights
Publication Abstract from PubMedBotulinum neurotoxins (BoNTs) are highly poisonous substances that are also effective medicines. Accidental BoNT poisoning often occurs through ingestion of Clostridium botulinum-contaminated food. Here, we present the crystal structure of a BoNT in complex with a clostridial nontoxic nonhemagglutinin (NTNHA) protein at 2.7 angstroms. Biochemical and functional studies show that NTNHA provides large and multivalent binding interfaces to protect BoNT from gastrointestinal degradation. Moreover, the structure highlights key residues in BoNT that regulate complex assembly in a pH-dependent manner. Collectively, our findings define the molecular mechanisms by which NTNHA shields BoNT in the hostile gastrointestinal environment and releases it upon entry into the circulation. These results will assist in the design of small molecules for inhibiting oral BoNT intoxication and of delivery vehicles for oral administration of biologics. Botulinum neurotoxin is shielded by NTNHA in an interlocked complex.,Gu S, Rumpel S, Zhou J, Strotmeier J, Bigalke H, Perry K, Shoemaker CB, Rummel A, Jin R Science. 2012 Feb 24;335(6071):977-81. PMID:22363010[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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