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| | ==Crystal structure of HA70 (HA3) subcomponent of Clostridium botulinum type C progenitor toxin in complex with alpha 2-3-sialyllactose== | | ==Crystal structure of HA70 (HA3) subcomponent of Clostridium botulinum type C progenitor toxin in complex with alpha 2-3-sialyllactose== |
| - | <StructureSection load='4en6' size='340' side='right' caption='[[4en6]], [[Resolution|resolution]] 2.56Å' scene=''> | + | <StructureSection load='4en6' size='340' side='right'caption='[[4en6]], [[Resolution|resolution]] 2.56Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4en6]] is a 2 chain structure with sequence from [http://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=4EN6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EN6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4en6]] 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=4EN6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EN6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</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=4en6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4en6 OCA], [https://pdbe.org/4en6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4en6 RCSB], [https://www.ebi.ac.uk/pdbsum/4en6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4en6 ProSAT]</span></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2zs6|2zs6]], [[2zoe|2zoe]], [[4en7|4en7]], [[4en8|4en8]], [[4en9|4en9]]</td></tr>
| + | |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HA-70 ([http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4en6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4en6 OCA], [http://pdbe.org/4en6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4en6 RCSB], [http://www.ebi.ac.uk/pdbsum/4en6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4en6 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [[https://www.uniprot.org/uniprot/HA70C_CBCP HA70C_CBCP]] The hemagglutinin (HA) component of the progenitor toxin protects the structural integrity of botulinum neurotoxin; may increase internalization of the neurotoxin into the bloodstream of the host (PubMed:9421908). The HA component is involved in binding to the upper small intestine through interactions with glycolipids and glycoproteins containing sialic acid moieties (Probable). Whole protein and the HA-53 chain (but not the HA-22-23 chain) bind to bovine mucin; if the mucin is pretreated with neuraminidase (removes the terminal sialic acid of glycoconjugates) mucin binding is decreased (PubMed:19071137). Has higher affinity for alpha-2,3-sialylated oligosaccharides than alpha-2-6 sialylated oligosaccharides (PubMed:22684008).<ref>PMID:19071137</ref> <ref>PMID:22684008</ref> <ref>PMID:9421908</ref> <ref>PMID:9421908</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Hemagglutinin|Hemagglutinin]] | + | *[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus botulinus van ermengem 1896]] | + | [[Category: Clostridium botulinum]] |
| - | [[Category: Kamitori, S]] | + | [[Category: Large Structures]] |
| - | [[Category: Nishikawa, A]] | + | [[Category: Kamitori S]] |
| - | [[Category: Tonozuka, T]] | + | [[Category: Nishikawa A]] |
| - | [[Category: Yamashita, S]] | + | [[Category: Tonozuka T]] |
| - | [[Category: Yoshida, H]] | + | [[Category: Yamashita S]] |
| - | [[Category: Carbohydrate/sugar binding]]
| + | [[Category: Yoshida H]] |
| - | [[Category: Sugar binding protein]]
| + | |
| Structural highlights
Function
[HA70C_CBCP] The hemagglutinin (HA) component of the progenitor toxin protects the structural integrity of botulinum neurotoxin; may increase internalization of the neurotoxin into the bloodstream of the host (PubMed:9421908). The HA component is involved in binding to the upper small intestine through interactions with glycolipids and glycoproteins containing sialic acid moieties (Probable). Whole protein and the HA-53 chain (but not the HA-22-23 chain) bind to bovine mucin; if the mucin is pretreated with neuraminidase (removes the terminal sialic acid of glycoconjugates) mucin binding is decreased (PubMed:19071137). Has higher affinity for alpha-2,3-sialylated oligosaccharides than alpha-2-6 sialylated oligosaccharides (PubMed:22684008).[1] [2] [3] [4]
Publication Abstract from PubMed
Clostridium botulinum produces the botulinum neurotoxin, forming a large complex as progenitor toxins in association with non-toxic non-hemagglutinin and/or several different hemagglutinin (HA) subcomponents, HA33, HA17 and HA70, which bind to carbohydrate of glycoproteins from epithelial cells in the infection process. To elucidate the carbohydrate recognition mechanism of HA70, X-ray structures of HA70 from type C toxin (HA70/C) in complexes with sialylated oligosaccharides were determined, and a binding assay by the glycoconjugate microarray was performed. These results suggested that HA70/C can recognize both alpha2-3- and alpha2-6-sialylated oligosaccharides, and that it has a higher affinity for alpha2-3-sialylated oligosaccharides.
Carbohydrate recognition mechanism of HA70 from Clostridium botulinum deduced from X-ray structures in complexes with sialylated oligosaccharides.,Yamashita S, Yoshida H, Uchiyama N, Nakakita Y, Nakakita S, Tonozuka T, Oguma K, Nishikawa A, Kamitori S FEBS Lett. 2012 Jul 30;586(16):2404-10. doi: 10.1016/j.febslet.2012.05.055. Epub , 2012 Jun 7. PMID:22684008[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Nakamura T, Kotani M, Tonozuka T, Ide A, Oguma K, Nishikawa A. Crystal structure of the HA3 subcomponent of Clostridium botulinum type C progenitor toxin. J Mol Biol. 2009 Jan 30;385(4):1193-206. Epub 2008 Nov 27. PMID:19071137 doi:10.1016/j.jmb.2008.11.039
- ↑ Yamashita S, Yoshida H, Uchiyama N, Nakakita Y, Nakakita S, Tonozuka T, Oguma K, Nishikawa A, Kamitori S. Carbohydrate recognition mechanism of HA70 from Clostridium botulinum deduced from X-ray structures in complexes with sialylated oligosaccharides. FEBS Lett. 2012 Jul 30;586(16):2404-10. doi: 10.1016/j.febslet.2012.05.055. Epub , 2012 Jun 7. PMID:22684008 doi:10.1016/j.febslet.2012.05.055
- ↑ Fujinaga Y, Inoue K, Watanabe S, Yokota K, Hirai Y, Nagamachi E, Oguma K. The haemagglutinin of Clostridium botulinum type C progenitor toxin plays an essential role in binding of toxin to the epithelial cells of guinea pig small intestine, leading to the efficient absorption of the toxin. Microbiology (Reading). 1997 Dec;143 ( Pt 12):3841-3847. doi:, 10.1099/00221287-143-12-3841. PMID:9421908 doi:http://dx.doi.org/10.1099/00221287-143-12-3841
- ↑ Fujinaga Y, Inoue K, Watanabe S, Yokota K, Hirai Y, Nagamachi E, Oguma K. The haemagglutinin of Clostridium botulinum type C progenitor toxin plays an essential role in binding of toxin to the epithelial cells of guinea pig small intestine, leading to the efficient absorption of the toxin. Microbiology (Reading). 1997 Dec;143 ( Pt 12):3841-3847. doi:, 10.1099/00221287-143-12-3841. PMID:9421908 doi:http://dx.doi.org/10.1099/00221287-143-12-3841
- ↑ Yamashita S, Yoshida H, Uchiyama N, Nakakita Y, Nakakita S, Tonozuka T, Oguma K, Nishikawa A, Kamitori S. Carbohydrate recognition mechanism of HA70 from Clostridium botulinum deduced from X-ray structures in complexes with sialylated oligosaccharides. FEBS Lett. 2012 Jul 30;586(16):2404-10. doi: 10.1016/j.febslet.2012.05.055. Epub , 2012 Jun 7. PMID:22684008 doi:10.1016/j.febslet.2012.05.055
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