4EN8
Crystal structure of HA70 (HA3) subcomponent of Clostridium botulinum type C progenitor toxin in complex with alpha 2-6-sialyllactose
Summary for 4EN8
| Entry DOI | 10.2210/pdb4en8/pdb |
| Related | 2ZOE 2ZS6 4EN6 4EN7 4EN9 |
| Related PRD ID | PRD_900066 |
| Descriptor | Hemagglutinin components HA-22/23/53, N-acetyl-alpha-neuraminic acid-(2-6)-beta-D-galactopyranose-(1-4)-beta-D-glucopyranose, (4R)-2-METHYLPENTANE-2,4-DIOL, ... (5 entities in total) |
| Functional Keywords | carbohydrate/sugar binding, sugar binding protein |
| Biological source | Clostridium botulinum More |
| Total number of polymer chains | 2 |
| Total formula weight | 74608.81 |
| Authors | Yamashita, S.,Yoshida, H.,Tonozuka, T.,Nishikawa, A.,Kamitori, S. (deposition date: 2012-04-12, release date: 2012-06-06, Last modification date: 2023-11-08) |
| Primary citation | 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., 586:2404-2410, 2012 Cited by PubMed Abstract: 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 α2-3- and α2-6-sialylated oligosaccharides, and that it has a higher affinity for α2-3-sialylated oligosaccharides. PubMed: 22684008DOI: 10.1016/j.febslet.2012.05.055 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
Download full validation report






