Conformational dynamics of the anthrax lethal factor catalytic center.
Anthrax lethal factor (LF) is a zinc-metalloprotease that together with the protective antigen constitutes anthrax lethal toxin, which is the most prominent virulence factor of the anthrax disease. The solution nuclear magnetic resonance and in silico conformational dynamics of the 105 C-terminal residues of the LF catalytic core domain in its apo form are described here. The polypeptide adopts a compact structure even in the absence of the Zn(2+) cofactor, while the 40 N-terminal residues comprising the metal ligands and residues that participate in substrate and inhibitor recognition exhibit more flexibility than the C-terminal region.
Department of Pharmacy, University of Patras, GR-26504 Patras, Greece.
Georgios A
GA
Dalkas
Christos T
CT
Chasapis
Petros V
PV
Gkazonis
Detlef
D
Bentrop
Georgios A
GA
Spyroulias
D000881:Anthrax / Q000382:microbiology*; D000942:Antigens, Bacterial / Q000737:chemistry*; D001408:Bacillus anthracis / Q000737:chemistry*; D001427:Bacterial Toxins / Q000737:chemistry*; D020134:Catalytic Domain; D006801:Humans; D056004:Molecular Dynamics Simulation; D019906:Nuclear Magnetic Resonance, Biomolecular
D000942:Antigens, Bacterial; D001427:Bacterial Toxins; C030325:anthrax toxin