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Updated: Jul 15, 2026

Recombinant Protein Expression, Crystallization, and Biophysical Studies of a Bacillus-conserved Nucleotide Pyrophosphorylase, BcMazG
Published on: May 16, 2017
Mutation of the zinc-binding metalloprotease motif affects Bacteroides fragilis toxin activity but does not affect
Augusto A Franco1, Simy L Buckwold, Jai W Shin
1Division of Infectious Diseases, Johns Hopkins University School of Medicine, Ross Bldg., Rm. 1167, 1147B Rutland Ave., Baltimore, MD 21205, USA. afranco@jhem.jhmi.edu
Abstract:
To evaluate the role of the zinc-binding metalloprotease in Bacteroides fragilis toxin (BFT) processing and activity, the zinc-binding consensus sequences (H348, E349, H352, G355, H358, and M366) were mutated by site-directed-mutagenesis. Our results indicated that single point mutations in the zinc-binding metalloprotease motif do not affect BFT processing but do reduce or eliminate BFT biologic activity in vitro.
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