Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
The structure of the neurotoxin-associated protein HA33/A from Clostridium botulinum suggests a reoccurring beta-trefoil fold in the progenitor toxin complex.,Arndt JW, Gu J, Jaroszewski L, Schwarzenbacher R, Hanson MA, Lebeda FJ, Stevens RC J Mol Biol. 2005 Mar 4;346(4):1083-93. Epub 2005 Jan 20. PMID:15701519[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Arndt JW, Gu J, Jaroszewski L, Schwarzenbacher R, Hanson MA, Lebeda FJ, Stevens RC. 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. 2005 Mar 4;346(4):1083-93. Epub 2005 Jan 20. PMID:15701519 doi:10.1016/j.jmb.2004.12.039
