3fii: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Crystal structure of Clostridium botulinum neurotoxin serotype F catalytic domain with an inhibitor (inh2)== | ==Crystal structure of Clostridium botulinum neurotoxin serotype F catalytic domain with an inhibitor (inh2)== | ||
<StructureSection load='3fii' size='340' side='right' caption='[[3fii]], [[Resolution|resolution]] 2.17Å' scene=''> | <StructureSection load='3fii' size='340' side='right'caption='[[3fii]], [[Resolution|resolution]] 2.17Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3fii]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3fii]] is a 2 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=3FII OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FII 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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=00C:3-SULFO-D-ALANINE'>00C</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=00C:3-SULFO-D-ALANINE'>00C</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2a8a|2a8a]], [[2a97|2a97]], [[3fie|3fie]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2a8a|2a8a]], [[2a97|2a97]], [[3fie|3fie]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bonT/F ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bonT/F ([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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Bontoxilysin Bontoxilysin], with EC number [https://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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3fii FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fii OCA], [https://pdbe.org/3fii PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fii RCSB], [https://www.ebi.ac.uk/pdbsum/3fii PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fii ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/VAMP2_HUMAN VAMP2_HUMAN]] Involved in the targeting and/or fusion of transport vesicles to their target membrane. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 34: | Line 34: | ||
==See Also== | ==See Also== | ||
*[[Botulinum neurotoxin|Botulinum neurotoxin]] | *[[Botulinum neurotoxin 3D structures|Botulinum neurotoxin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 41: | Line 41: | ||
[[Category: Bacillus botulinus van ermengem 1896]] | [[Category: Bacillus botulinus van ermengem 1896]] | ||
[[Category: Bontoxilysin]] | [[Category: Bontoxilysin]] | ||
[[Category: Large Structures]] | |||
[[Category: Agarwal, R]] | [[Category: Agarwal, R]] | ||
[[Category: Swaminathan, S]] | [[Category: Swaminathan, S]] | ||
Revision as of 11:02, 2 March 2022
Crystal structure of Clostridium botulinum neurotoxin serotype F catalytic domain with an inhibitor (inh2)Crystal structure of Clostridium botulinum neurotoxin serotype F catalytic domain with an inhibitor (inh2)
Structural highlights
Function[VAMP2_HUMAN] Involved in the targeting and/or fusion of transport vesicles to their target membrane. 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 PubMedClostridium botulinum neurotoxins (BoNTs) cleave neuronal proteins responsible for neurotransmitter release, causing the neuroparalytic disease botulism. BoNT serotypes B, D, F and G cleave and inactivate vesicle-associated membrane protein (VAMP), each at a unique peptide bond. The specificity of BoNTs depends on the mode of substrate recognition. We have investigated the mechanism of substrate recognition of BoNT F by determining the crystal structures of its complex with two substrate-based inhibitors, VAMP 22-58/Gln58D-cysteine and 27-58/Gln58D-cysteine. The inhibitors bind to BoNT F in the canonical direction (as seen for BoNTs A and E substrates) but are positioned specifically via three major exosites away from the active site. The cysteine sulfur of the inhibitors interacts with the zinc and exists as sulfinic acid in the inhibitor VAMP 27-58/Gln58D-cysteine. Arg133 and Arg171, which form part of two separate exosites, are crucial for substrate binding and catalysis. Mode of VAMP substrate recognition and inhibition of Clostridium botulinum neurotoxin F.,Agarwal R, Schmidt JJ, Stafford RG, Swaminathan S Nat Struct Mol Biol. 2009 Jul;16(7):789-94. Epub 2009 Jun 21. PMID:19543288[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||||||||