3azv: Difference between revisions
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<StructureSection load='3azv' size='340' side='right'caption='[[3azv]], [[Resolution|resolution]] 3.10Å' scene=''> | <StructureSection load='3azv' size='340' side='right'caption='[[3azv]], [[Resolution|resolution]] 3.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3azv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3azv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_botulinum Clostridium botulinum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AZV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AZV FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3azv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3azv OCA], [https://pdbe.org/3azv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3azv RCSB], [https://www.ebi.ac.uk/pdbsum/3azv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3azv ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3azv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3azv OCA], [https://pdbe.org/3azv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3azv RCSB], [https://www.ebi.ac.uk/pdbsum/3azv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3azv ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9LBR1_CLOBO Q9LBR1_CLOBO] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Clostridium botulinum]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Kozaki | [[Category: Kozaki S]] | ||
[[Category: Nakamura | [[Category: Nakamura K]] | ||
[[Category: Nuemket | [[Category: Nuemket N]] | ||
[[Category: Tanaka | [[Category: Tanaka I]] | ||
[[Category: Tanaka | [[Category: Tanaka Y]] | ||
[[Category: Tsuji | [[Category: Tsuji T]] | ||
[[Category: Tsukamoto | [[Category: Tsukamoto K]] | ||
[[Category: Yao | [[Category: Yao M]] | ||
Latest revision as of 11:50, 11 October 2023
Crystal structure of the receptor binding domainCrystal structure of the receptor binding domain
Structural highlights
FunctionPublication Abstract from PubMedClostridium botulinum type D strain OFD05, which produces the D/C mosaic neurotoxin, was isolated from cattle killed by the recent botulism outbreak in Japan. The D/C mosaic neurotoxin is the most toxic of the botulinum neurotoxins (BoNT) characterized to date. Here, we determined the crystal structure of the receptor binding domain of BoNT from strain OFD05 in complex with 3'-sialyllactose at a resolution of 3.0A. In the structure, an electron density derived from the 3'-sialyllactose was confirmed at the cleft in the C-terminal subdomain. Alanine site-directed mutagenesis showed the significant contribution of the residues surrounding the cleft to ganglioside recognition. In addition, a loop adjoining the cleft also plays an important role in ganglioside recognition. In contrast, little effect was observed when the residues located around the surface previously identified as the protein receptor binding site in other BoNTs were substituted. The results of cell binding analysis of the mutants were significantly correlated with the ganglioside binding properties. Based on these observations, a cell binding mechanism of BoNT from strain OFD05 is proposed, which involves cooperative contribution of two ganglioside binding sites. Structural and mutational analyses of the receptor binding domain of botulinum D/C mosaic neurotoxin: insight into the ganglioside binding mechanism.,Nuemket N, Tanaka Y, Tsukamoto K, Tsuji T, Nakamura K, Kozaki S, Yao M, Tanaka I Biochem Biophys Res Commun. 2011 Jul 29;411(2):433-9. Epub 2011 Jul 2. PMID:21749855[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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