4YU5

Crystal structure of selenomethionine variant of Bacillus anthracis immune inhibitor A2 peptidase zymogen

Summary for 4YU5

• Entry DOI: 10.2210/pdb4yu5/pdb
• Related: 4YU6
• Descriptor: Immune inhibitor A, metalloprotease, ZINC ION, CALCIUM ION, ... (7 entities in total)
• Functional Keywords: hydrolase, metallopeptidase, metzincin
• Biological source: Bacillus cereus var. anthracis (strain CI)
• Total number of polymer chains: 2
• Total formula weight: 169734.74

Authors

Arolas, J.L.,Goulas, T.,Gomis-Ruth, F.X. (deposition date: 2015-03-18, release date: 2015-10-28, Last modification date: 2024-11-06)

Primary citation

Arolas, J.L.,Goulas, T.,Pomerantsev, A.P.,Leppla, S.H.,Gomis-Ruth, F.X.
Structural Basis for Latency and Function of Immune Inhibitor A Metallopeptidase, a Modulator of the Bacillus anthracis Secretome.
Structure, 24:25-36, 2016

PubMed 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.

PubMed: 26745529
DOI: 10.1016/j.str.2015.10.015

Experimental method

X-RAY DIFFRACTION (2.9 Å)