title: The structure of the neurotoxin-associated protein HA33/A from Clostridium botulinum suggests a reoccurring beta-trefoil fold in the progenitor toxin complex.
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.
authors.affiliation: Department of Molecular Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla, CA 92037, USA.
authors.forename: Joseph W
authors.initials: JW
authors.lastname: Arndt
authors.forename: Jenny
authors.initials: J
authors.lastname: Gu
authors.forename: Lukasz
authors.initials: L
authors.lastname: Jaroszewski
authors.forename: Robert
authors.initials: R
authors.lastname: Schwarzenbacher
authors.forename: Michael A
authors.initials: MA
authors.lastname: Hanson
authors.forename: Frank J
authors.initials: FJ
authors.lastname: Lebeda
authors.forename: Raymond C
authors.initials: RC
authors.lastname: Stevens
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism*; D001665:Binding Sites; D050260:Carbohydrate Metabolism; D003014:Clostridium botulinum / Q000737:chemistry*; D017124:Conserved Sequence; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009498:Neurotoxins / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D017510:Protein Folding; D016415:Sequence Alignment
chemical_list: D001426:Bacterial Proteins; D009498:Neurotoxins