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3azw

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==Crystal structure of the receptor binding domain==
==Crystal structure of the receptor binding domain==
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<StructureSection load='3azw' size='340' side='right' caption='[[3azw]], [[Resolution|resolution]] 2.99&Aring;' scene=''>
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<StructureSection load='3azw' size='340' side='right'caption='[[3azw]], [[Resolution|resolution]] 2.99&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3azw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_botulinum Clostridium botulinum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AZW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AZW FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3azw]] 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=3AZW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AZW FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.99&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3n7l|3n7l]], [[3azv|3azv]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bont ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1491 Clostridium botulinum])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3azw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3azw OCA], [https://pdbe.org/3azw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3azw RCSB], [https://www.ebi.ac.uk/pdbsum/3azw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3azw ProSAT]</span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3azw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3azw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3azw RCSB], [http://www.ebi.ac.uk/pdbsum/3azw PDBsum]</span></td></tr>
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</table>
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<table>
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== Function ==
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<div style="background-color:#fffaf0;">
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[https://www.uniprot.org/uniprot/Q9LBR1_CLOBO Q9LBR1_CLOBO]
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== Publication Abstract from PubMed ==
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Clostridium 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.
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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<ref>PMID:21749855</ref>
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Clostridium botulinum]]
[[Category: Clostridium botulinum]]
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[[Category: Kozaki, S.]]
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[[Category: Large Structures]]
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[[Category: Nakamura, K.]]
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[[Category: Kozaki S]]
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[[Category: Nuemket, N.]]
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[[Category: Nakamura K]]
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[[Category: Tanaka, I.]]
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[[Category: Nuemket N]]
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[[Category: Tanaka, Y.]]
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[[Category: Tanaka I]]
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[[Category: Tsuji, T.]]
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[[Category: Tanaka Y]]
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[[Category: Tsukamoto, K.]]
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[[Category: Tsuji T]]
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[[Category: Yao, M.]]
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[[Category: Tsukamoto K]]
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[[Category: Beta-sheet jellyroll fold]]
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[[Category: Yao M]]
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[[Category: Beta-trefoil fold]]
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[[Category: Toxin]]
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Current revision

Crystal structure of the receptor binding domain

PDB ID 3azw

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