Reference : Differential Functionalities of Amphiphilic Peptide Segments of the Cell-Septation Pe...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/13171
Differential Functionalities of Amphiphilic Peptide Segments of the Cell-Septation Penicillin-Binding Protein 3 of Escherichia Coli
English
Marrec-Fairley, Monique [Université de Liège - ULg > > Centre d'Ingénierie des Protéines > >]
Piette, André mailto [Université de Liège - ULg > > Centre d'Ingénierie des Protéines > >]
Gallet, Xavier [Faculté Universitaire des Sciences Agronomiques de Gembloux - FUSAGx > > > > > >]
Brasseur, Robert mailto [Faculté Universitaire des Sciences Agronomiques de Gembloux - FUSAGx > > > >]
Hara, Hirochi [Saitama University Japan > > Biochemistry and Molecular Biology > > >]
Fraipont, Claudine mailto [Université de Liège - ULg > > Centre d'Ingénierie des Protéines > >]
Ghuysen, Jean-Marie [Université de Liège - ULg > > > Centre d'Ingénierie des Protéines > > >]
Nguyen-Disteche, Martine mailto [Université de Liège - ULg > > Centre d'Ingénierie des Protéines > > >]
Sep-2000
Molecular Microbiology
Blackwell Publishing
37
5
1019-1031
Yes (verified by ORBi)
International
0950-382X
1365-2958
Oxford
United Kingdom
[en] PBP3 ; divisome
[en] The class B M1-V577 penicillin-binding protein (PBP) 3 of Escherichia coli consists of a M1-L39 membrane anchor (bearing a cytosolic tail) that is linked via a G40-S70 intervening peptide to an R71-I236 non-catalytic module (containing the conserved motifs 1-3) itself linked via motif 4 to a D237-V577 catalytic module (containing the conserved motifs 5-7 of the penicilloyl serine transferases superfamily). It has been proposed that during cell septation the peptidoglycan crosslinking activity of the acyl transferase module of PBP3 is regulated by the associated M1-I236 polypeptide itself in interaction with other components of the divisome. The fold adopted by the R71-V577 polypeptide of PBP3 has been modelled by reference to the corresponding R76-S634 polypeptide of the class B Streptococcus pneumoniae PBP2x. Based on these data and the results of site-directed mutagenesis of motifs 1-3 and of peptide segments of high amphiphilicity (identified from hydrophobic moment plots), the M1-I236 polypeptide of PBP3 appears to be precisely designed to work in the way proposed. The membrane anchor and the G40-S70 sequence (containing the G57-Q66 peptide segment) upstream from the non-catalytic module have the information ensuring that PBP3 undergoes proper insertion within the divisome at the cell septation site. Motif 1 and the I74-L82 overlapping peptide segment, motif 2 and the H160-G172 overlapping peptide segment, and the G188-D197 motif 3 are located at or close to the intermodule junction. They contain the information ensuring that PBP3 folds correctly and the acyl transferase catalytic centre adopts the active configuration. The E206-V217 peptide segment is exposed at the surface of the non-catalytic module. It has the information ensuring that PBP3 fulfils its cell septation activity within the fully complemented divisome.
Centre d'Ingénierie des Protéines - CIP
Researchers ; Professionals
http://hdl.handle.net/2268/13171

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