Structural highlights
Publication Abstract from PubMed
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.
Conformational dynamics of the anthrax lethal factor catalytic center.,Dalkas GA, Chasapis CT, Gkazonis PV, Bentrop D, Spyroulias GA Biochemistry. 2010 Dec 28;49(51):10767-9. Epub 2010 Dec 3. PMID:21121613[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Dalkas GA, Chasapis CT, Gkazonis PV, Bentrop D, Spyroulias GA. Conformational dynamics of the anthrax lethal factor catalytic center. Biochemistry. 2010 Dec 28;49(51):10767-9. Epub 2010 Dec 3. PMID:21121613 doi:10.1021/bi1017792