4XM7

Anthrax toxin lethal factor with ligand-induced binding pocket

Summary for 4XM7

• Entry DOI: 10.2210/pdb4xm7/pdb
• Related: 1YQY 4PKQ 4PKR 4PKS 4PKT 4PKU 4PKV 4PKW 4WF6 4XM6 4XM8
• Descriptor: Lethal factor, N~2~-[(4-fluoro-3-methoxyphenyl)sulfonyl]-N-hydroxy-N~2~-(2-methylpropyl)-D-valinamide, ZINC ION, ... (5 entities in total)
• Functional Keywords: anthrax toxin, lethal factor, metalloproteinase, metalloprotease, structural dynamics, ligand-induced conformational change, toxin, hydrolase
• Biological source: Bacillus anthracis
• Total number of polymer chains: 1
• Total formula weight: 60939.97

Authors

Maize, K.M.,Finzel, B.C. (deposition date: 2015-01-14, release date: 2015-11-11, Last modification date: 2023-09-27)

Primary citation

Maize, K.M.,Kurbanov, E.K.,Johnson, R.L.,Amin, E.A.,Finzel, B.C.
Ligand-induced expansion of the S1' site in the anthrax toxin lethal factor.
Febs Lett., 589:3836-3841, 2015

PubMed Abstract: The Bacillus anthracis lethal factor (LF) is one component of a tripartite exotoxin partly responsible for persistent anthrax cytotoxicity after initial bacterial infection. Inhibitors of the zinc metalloproteinase have been investigated as potential therapeutic agents, but LF is a challenging target because inhibitors lack sufficient selectivity or possess poor pharmaceutical properties. These structural studies reveal an alternate conformation of the enzyme, induced upon binding of specific inhibitors, that opens a previously unobserved deep pocket termed S1'(∗) which might afford new opportunities to design selective inhibitors that target this subsite.

PubMed: 26578066
DOI: 10.1016/j.febslet.2015.11.005

Experimental method

X-RAY DIFFRACTION (2.7 Å)