PMID:10972821
| Citation |
Marrec-Fairley, M, Piette, A, Gallet, X, Brasseur, R, Hara, H, Fraipont, C, Ghuysen, JM and Nguyen-Distèche, M (2000) Differential functionalities of amphiphilic peptide segments of the cell-septation penicillin-binding protein 3 of Escherichia coli. Mol. Microbiol. 37:1019-31 |
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| Abstract |
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. |
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| Keywords |
Amino Acid Motifs; Amino Acid Sequence; Bacterial Proteins; Binding Sites; Carrier Proteins; Escherichia coli/chemistry; Escherichia coli Proteins; Hexosyltransferases/chemistry; Hexosyltransferases/genetics; Hexosyltransferases/physiology; Molecular Sequence Data; Multienzyme Complexes/chemistry; Multienzyme Complexes/genetics; Multienzyme Complexes/physiology; Muramoylpentapeptide Carboxypeptidase; Penicillin-Binding Proteins; Peptides/chemistry; Peptides/genetics; Peptides/physiology; Peptidoglycan Glycosyltransferase; Peptidyl Transferases/chemistry; Peptidyl Transferases/genetics; Peptidyl Transferases/physiology; Structure-Activity Relationship |
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