Structural highlights
4en6 is a 2 chain structure with sequence from "bacillus_botulinus"_van_ermengem_1896 "bacillus botulinus" van ermengem 1896. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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Ligands: | , , |
NonStd Res: | |
Related: | 2zs6, 2zoe, 4en7, 4en8, 4en9 |
Gene: | HA-70 ("Bacillus botulinus" van Ermengem 1896) |
Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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