Reference : Crystal structure of BRL 42715, C6-(N1-methyl-1,2,3-triazolylmethylene)penem, in complex...

	Document type :	Scientific journals : Article
	Discipline(s) :	Life sciences : Biochemistry, biophysics & molecular biology
	To cite this reference:	http://hdl.handle.net/2268/78083

Title :	Crystal structure of BRL 42715, C6-(N1-methyl-1,2,3-triazolylmethylene)penem, in complex with Enterobacter cloacae 908R beta-lactamase: evidence for a stereoselective mechanism from docking studies.
Language :	English
Author, co-author :	Michaux, Catherine [> > > >]
	Charlier, Paulette [Université de Liège - ULg > Département des sciences de la vie > Cristallographie des macromolécules biologiques >]
	Frère, Jean-Marie [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
	Wouters, Johan [> > > >]
Publication date :	2005
Journal title :	Journal of the American Chemical Society
Publisher :	American Chemical Society
Volume :	127
Issue/season :	10
Pages :	3262-3
Audience :	International
ISSN :	0002-7863
e-ISSN :	1520-5126
City :	Washington
Country :	DC
Keywords :	[en] Crystallography, X-Ray ; Enterobacter cloacae/enzymology ; Lactams/chemistry/metabolism ; Models, Molecular ; Stereoisomerism ; Thermodynamics ; beta-Lactamases/chemistry/metabolism
Abstract :	[en] BRL 42715, C6-(N1-methyl-1,2,3-triazolylmethylene)penem, is an active-site-directed inactivator of bacterial beta-lactamases. The crystal structure of Enterobacter cloacae 908R class C beta-lactamase in complex with BRL 42715, docking, and energy minimization studies explain stereoselectivity of the binding of C6-(heterocyclic methylene)penems against class C beta-lactamase.
Permalink :	http://hdl.handle.net/2268/78083
DOI :	10.1021/ja0426241

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