Reference : Crystal structure of the Actinomadura R39 DD-peptidase reveals new domains in penicil...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/78081
Crystal structure of the Actinomadura R39 DD-peptidase reveals new domains in penicillin-binding proteins.
English
Sauvage, Eric mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Herman, Raphaël mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Petrella, Stephanie [Université Pierre et Marie Curie, Paris France > > > > LRMA, INSERM U655 > >]
Duez, Colette mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Bouillenne, Fabrice mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Frère, Jean-Marie mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Charlier, Paulette mailto [Université de Liège - ULg > Département des sciences de la vie > Cristallographie des macromolécules biologiques >]
2005
Journal of Biological Chemistry
American Society for Biochemistry and Molecular Biology
280
35
31249-56
Yes (verified by ORBi)
International
0021-9258
1083-351X
Baltimore
MD
[en] Actinomycetales/chemistry ; Bacterial Proteins/chemistry/metabolism ; Cephalosporins/chemistry/metabolism ; Cobalt/chemistry ; Crystallography, X-Ray ; Indicators and Reagents/chemistry/metabolism ; Models, Molecular ; Penicillins/chemistry/metabolism ; Protein Structure, Tertiary ; Serine-Type D-Ala-D-Ala Carboxypeptidase/chemistry/metabolism
[en] Actinomadura sp. R39 produces an exocellular DD-peptidase/penicillin-binding protein (PBP) whose primary structure is similar to that of Escherichia coli PBP4. It is characterized by a high beta-lactam-binding activity (second order rate constant for the acylation of the active site serine by benzylpenicillin: k2/K = 300 mm(-1) s(-1)). The crystal structure of the DD-peptidase from Actinomadura R39 was solved at a resolution of 1.8 angstroms by single anomalous dispersion at the cobalt resonance wavelength. The structure is composed of three domains: a penicillin-binding domain similar to the penicillin-binding domain of E. coli PBP5 and two domains of unknown function. In most multimodular PBPs, additional domains are generally located at the C or N termini of the penicillin-binding domain. In R39, the other two domains are inserted in the penicillin-binding domain, between the SXXK and SXN motifs, in a manner similar to "Matryoshka dolls." One of these domains is composed of a five-stranded beta-sheet with two helices on one side, and the other domain is a double three-stranded beta-sheet inserted in the previous domain. Additionally, the 2.4-angstroms structure of the acyl-enzyme complex of R39 with nitrocefin reveals the absence of active site conformational change upon binding the beta-lactams.
Researchers
http://hdl.handle.net/2268/78081
also: http://hdl.handle.net/2268/5995
10.1074/jbc.M503271200

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