AI Article Synopsis
- The hemagglutinating protein HA33 from Clostridium botulinum plays a vital role in protecting, internalizing, and potentially activating the botulinum neurotoxin.
- The crystal structure of the HA33 from serotype A has been analyzed at a high resolution, revealing its unique domain layout and a site for carbohydrate recognition.
- Sequence comparisons of other components in the toxin complex indicate a common beta-trefoil fold present in many of them, including the neurotoxin BoNT/A and hemagglutinating proteins.
Article 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.
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| http://dx.doi.org/10.1016/j.jmb.2004.12.039 | DOI Listing |
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