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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-Rüth FX
Structure 24 25-36 (2016)
Cited: 4 times
EuropePMC logo PMID: 26745529

Abstract

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 ∼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 α-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.

Articles - 4yu6 mentioned but not cited (1)

  1. 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-Rüth FX. Structure 24 25-36 (2016)


Articles citing this publication (3)

  1. In silico characterization and structural modeling of bacterial metalloprotease of family M4. Hasan R, Rony MNH, Ahmed R. J Genet Eng Biotechnol 19 25 (2021)
  2. Feeding Anthrax: The Crystal Structure of Bacillus anthracis InhA Protease. Schacherl M, Baumann U. Structure 24 1-2 (2016)
  3. Extending the novel |ρ|-based phasing algorithm to the solution of anomalous scattering substructures from SAD data of protein crystals. Rius J, Torrelles X. Acta Crystallogr A Found Adv 78 473-481 (2022)


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