1j7n

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spinqualitylabelsall models 1j7n, resolution 2.3Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Anthrax Toxin Lethal factor

Overview

Lethal factor (LF) is a protein (relative molecular mass 90,000) that is, critical in the pathogenesis of anthrax. It is a highly specific protease, that cleaves members of the mitogen-activated protein kinase kinase, (MAPKK) family near to their amino termini, leading to the inhibition of, one or more signalling pathways. Here we describe the crystal structure of, LF and its complex with the N terminus of MAPKK-2. LF comprises four, domains: domain I binds the membrane-translocating component of anthrax, toxin, the protective antigen (PA); domains II, III and IV together create, a long deep groove that holds the 16-residue N-terminal tail of MAPKK-2, before cleavage. Domain II resembles the ADP-ribosylating toxin from, Bacillus cereus, but the active site has been mutated and recruited to, augment substrate recognition. Domain III is inserted into domain II, and, seems to have arisen from a repeated duplication of a structural element, of domain II. Domain IV is distantly related to the zinc metalloprotease, family, and contains the catalytic centre; it also resembles domain I. The, structure thus reveals a protein that has evolved through a process of, gene duplication, mutation and fusion, into an enzyme with high and, unusual specificity.

About this Structure

1J7N is a Single protein structure of sequence from Bacillus anthracis with SO4 and ZN as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of the anthrax lethal factor., Pannifer AD, Wong TY, Schwarzenbacher R, Renatus M, Petosa C, Bienkowska J, Lacy DB, Collier RJ, Park S, Leppla SH, Hanna P, Liddington RC, Nature. 2001 Nov 8;414(6860):229-33. PMID:11700563

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