2L0R

Conformational Dynamics of the Anthrax Lethal Factor Catalytic Center

Summary for 2L0R

Entry DOI	10.2210/pdb2l0r/pdb
Descriptor	Lethal factor (1 entity in total)
Functional Keywords	protein, anthrax lethal factor, catalytic domain, zn metalloprotease, bacillus anthracis, hydrolase, toxin
Biological source	Bacillus anthracis (anthrax)
Cellular location	Secreted: P15917
Total number of polymer chains	1
Total formula weight	12139.41
Authors	Dalkas, G.A.,Chasapis, C.T.,Gkazonis, P.V.,Bentrop, D.A.,Spyroulias, G.A. (deposition date: 2010-07-15, release date: 2010-12-22, Last modification date: 2024-05-01)
Primary citation	Dalkas, G.A.,Chasapis, C.T.,Gkazonis, P.V.,Bentrop, D.,Spyroulias, G.A. Conformational dynamics of the anthrax lethal factor catalytic center. Biochemistry, 49:10767-10769, 2010 Cited by PubMed Abstract: 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. PubMed: 21121613 DOI: 10.1021/bi1017792 PDB entries with the same primary citation
Experimental method	SOLUTION NMR

Structure validation