1QXM

Crystal structure of a hemagglutinin component (HA1) from type C Clostridium botulinum

Summary for 1QXM

• Entry DOI: 10.2210/pdb1qxm/pdb
• Descriptor: HA1, 1,2-ETHANEDIOL (3 entities in total)
• Functional Keywords: clostridium botulinum, hemagglutinin, ha1, trefoil, toxin
• Biological source: Clostridium botulinum D phage
• Total number of polymer chains: 2
• Total formula weight: 71533.17

Authors

Inoue, K.,Sobhany, M.,Transue, T.R.,Oguma, K.,Pedersen, L.C.,Negishi, M. (deposition date: 2003-09-08, release date: 2004-01-20, Last modification date: 2024-02-14)

Primary citation

Inoue, K.,Sobhany, M.,Transue, T.R.,Oguma, K.,Pedersen, L.C.,Negishi, M.
Structural analysis by X-ray crystallography and calorimetry of a haemagglutinin component (HA1) of the progenitor toxin from Clostridium botulinum.
Microbiology, 149:3361-3370, 2003

PubMed Abstract: Botulism food poisoning is caused primarily by ingestion of the Clostridium botulinum neurotoxin (BoNT). The 1300 amino acid BoNT forms a progenitor toxin (PTX) that, when associated with a number of other proteins, increases its oral toxicity by protecting it from the low pH of the stomach and from intestinal proteases. One of these associated proteins, HA1, has also been suggested to be involved with internalization of the toxin into the bloodstream by binding to oligosaccharides lining the intestine. Here is reported the crystal structure of HA1 from type C Clostridium botulinum at a resolution of 1.7 Angstrom. The protein consists of two beta-trefoil domains and bears structural similarities to the lectin B-chain from the deadly plant toxin ricin. Based on structural comparison to the ricin B-chain lactose-binding sites, residues of type A HA1 were selected and mutated. The D263A and N285A mutants lost the ability to bind carbohydrates containing galactose moieties, implicating these residues in carbohydrate binding.

PubMed: 14663070
DOI: 10.1099/mic.0.26586-0

Experimental method

X-RAY DIFFRACTION (1.7 Å)