Structural highlights
Publication Abstract from PubMed
Immune inhibitor A(InhA)-type metallopeptidases are potential virulence factors secreted by members of the Bacillus cereus group. Two paralogs from anthrax-causing Bacillus anthracis (BaInhA1 and BaInhA2) were shown to degrade host tissue proteins with broad substrate specificity. Analysis of their activation mechanism and the crystal structure of a zymogenic BaInhA2 variant revealed a approximately 750-residue four-domain structure featuring a pro-peptide, a catalytic domain, a domain reminiscent of viral envelope glycoproteins, and a MAM domain grafted into the latter. This domain, previously found only in eukaryotes, is required for proper protein expression in B. anthracis and evinces certain flexibility. Latency is uniquely modulated by the N-terminal segment of the pro-peptide, which binds the catalytic zinc through its alpha-amino group and occupies the primed side of the active-site cleft. The present results further our understanding of the modus operandi of an anthrax secretome regulator.
Structural Basis for Latency and Function of Immune Inhibitor A Metallopeptidase, a Modulator of the Bacillus anthracis Secretome.,Arolas JL, Goulas T, Pomerantsev AP, Leppla SH, Gomis-Ruth FX Structure. 2016 Jan 5;24(1):25-36. doi: 10.1016/j.str.2015.10.015. PMID:26745529[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Arolas JL, Goulas T, Pomerantsev AP, Leppla SH, Gomis-Ruth FX. Structural Basis for Latency and Function of Immune Inhibitor A Metallopeptidase, a Modulator of the Bacillus anthracis Secretome. Structure. 2016 Jan 5;24(1):25-36. doi: 10.1016/j.str.2015.10.015. PMID:26745529 doi:http://dx.doi.org/10.1016/j.str.2015.10.015
