Reference : Structural basis for the interaction of lactivicins with serine beta-lactamases.
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/78028
Structural basis for the interaction of lactivicins with serine beta-lactamases.
English
Brown, Tom Jr [> > > >]
Charlier, Paulette mailto [Université de Liège - ULg > Département des sciences de la vie > Cristallographie des macromolécules biologiques >]
Herman, Raphaël mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Schofield, Christopher J [> > > >]
Sauvage, Eric mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
2010
Journal of Medicinal Chemistry
American Chemical Society
53
15
5890-4
Yes (verified by ORBi)
International
0022-2623
1520-4804
Washington
DC
[en] Anti-Bacterial Agents/chemistry ; Bacillus/enzymology ; Crystallography, X-Ray ; Models, Molecular ; Molecular Structure ; Peptides/chemistry ; Serine/metabolism ; beta-Lactamases/chemistry/metabolism
[en] Lactivicin (LTV) is a natural non-beta-lactam antibiotic that inhibits penicillin-binding proteins and serine beta-lactamases. A crystal structure of a BS3-LTV complex reveals that, as for its reaction with PBPs, LTV reacts with the nucleophilic serine and that cycloserine and lactone rings of LTV are opened. This structure, together with reported structures of PBP1b with lactivicins, provides a basis for developing improved lactivicin-based gamma-lactam antibiotics.
http://hdl.handle.net/2268/78028
10.1021/jm100437u

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