http://www.cnr.it/ontology/cnr/individuo/prodotto/ID4049
Anthrax Lethal Factor Investigated by Molecular Simulations (Articolo in rivista)
- Type
- Label
- Anthrax Lethal Factor Investigated by Molecular Simulations (Articolo in rivista) (literal)
- Anno
- 2008-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1021/ct8001877 (literal)
- Alternative label
Hong, R; Magistrato, A; Carloni, P (2008)
Anthrax Lethal Factor Investigated by Molecular Simulations
in Journal of chemical theory and computation
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Hong, R; Magistrato, A; Carloni, P (literal)
- Pagina inizio
- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
- Note
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- [1] SISSA, ISAS, [2] CNR, INFM,Democritos Natl Simulat Ctr, I-34014 Trieste, Italy; [3] IIT, Trieste, Italy (literal)
- Titolo
- Anthrax Lethal Factor Investigated by Molecular Simulations (literal)
- Abstract
- \"The anthrax disease is caused by the lethal toxin secreted by the bacterium Bacillus anthracis. The toxin is a protein aggregate which contains a Zn-based hydrolase called anthrax Lethal Factor (LF). In this work, we investigate the structure of its Michaelis complex with an optimized MAPKK-like substrate using several computational methods including density functional theory, molecular dynamics, and coarse grained techniques. Our calculations suggest that (i) the presence of second-shell ligands is crucial for tuning the structure, energetics, and protonation state of the metal binding site, as found in other Zn-based enzymes; (ii) the nucleophilic agent is a Zn-bound water molecule; (iii) substrate binding to the active site groove is mainly stabilized by van der Waals interactions; (iv) the bonds most likely involved in the substrate hydrolysis are only mildly polarized by the protein scaffold; and (v) part of helix alpha 19, which is present in one solid state structure of LF (PDB: 1JKY), assumes a coiled conformation.\" (literal)
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