1YBI

Crystal structure of HA33A, a neurotoxin-associated protein from Clostridium botulinum type A

Summary for 1YBI

• Entry DOI: 10.2210/pdb1ybi/pdb
• Descriptor: non-toxin haemagglutinin HA34 (2 entities in total)
• Functional Keywords: beta-trefoil, toxin
• Biological source: Clostridium botulinum
• Total number of polymer chains: 2
• Total formula weight: 66503.66

Authors

Arndt, J.W.,Gu, J.,Jaroszewski, L.,Schwarzenbacher, R.,Hanson, M.,Lebeda, F.J.,Stevens, R.C. (deposition date: 2004-12-20, release date: 2005-02-22, Last modification date: 2023-08-23)

Primary citation

Arndt, J.W.,Gu, J.,Jaroszewski, L.,Schwarzenbacher, R.,Hanson, M.A.,Lebeda, F.J.,Stevens, R.C.
The Structure of the Neurotoxin-associated Protein HA33/A from Clostridium botulinum Suggests a Reoccurring beta-Trefoil Fold in the Progenitor Toxin Complex.
J.Mol.Biol., 346:1083-1093, 2005

PubMed Abstract: The hemagglutinating protein HA33 from Clostridium botulinum is associated with the large botulinum neurotoxin secreted complexes and is critical in toxin protection, internalization, and possibly activation. We report the crystal structure of serotype A HA33 (HA33/A) at 1.5 A resolution that contains a unique domain organization and a carbohydrate recognition site. In addition, sequence alignments of the other toxin complex components, including the neurotoxin BoNT/A, hemagglutinating protein HA17/A, and non-toxic non-hemagglutinating protein NTNHA/A, suggests that most of the toxin complex consists of a reoccurring beta-trefoil fold.

PubMed: 15701519
DOI: 10.1016/j.jmb.2004.12.039

Experimental method

X-RAY DIFFRACTION (1.5 Å)