Title: Comparison of the structural features of botulinum neurotoxin and NTNH, a non-toxic accessory protein of the progenitor complex
Authors: Kristine M. Krebs, Frank J. Lebeda
Addresses: Advanced Academic Program in Biotechnology, Johns Hopkins University, Baltimore, MD 21218, USA; Genome Technology Branch, National Human Genome Research Institute, National Institutes of Health, Bethesda, MD 20892, USA. ' Advanced Academic Program in Biotechnology, Johns Hopkins University, Baltimore, MD 21218, USA; Integrated Toxicology Division, US Army Medical Research Institute of Infectious Diseases, Fort Detrick, MD 21702-5011, USA
Abstract: The non-toxic, non-hemagglutinin (NTNH) protein occurs with the seven progenitor serotypes of the botulinum neurotoxins (BoNTs). Bioinformatic techniques predict that the N- and C-termini of NTNH have the same folds as the corresponding domains of BoNT. In contrast, the sequence pattern for zinc-binding in the catalytic domain of BoNT is absent in NTNH. The intermediate domain of NTNH is predicted to have neither the coiled-coil nor the hydrophobic characteristics of the corresponding region of BoNT. BoNT and NTNH are hypothesised to have diverged in their amino acid sequences from a common ancestor which accounts for their structural and functional differences. [Received 24 October 2007; Accepted 21 November 2007]
Keywords: chimera; coiled coil; hydrophobicity; mosaic; protein domains; protein folds; sequence alignment; botulinum neurotoxins; BoNT; botulism; bioinformatics; non-toxic non-hemagglutinin; NTNH protein; amino acid sequences.
The Botulinum Journal, 2008 Vol.1 No.1, pp.116 - 134
Published online: 25 Jun 2008 *Full-text access for editors Access for subscribers Purchase this article Comment on this article