PMID:9371419
| Citation |
Siligardi, G, Harris, F and Phoenix, DA (1997) Alpha-helical conformation in the C-terminal anchoring domains of E. coli penicillin-binding proteins 4, 5 and 6. Biochim. Biophys. Acta 1329:278-84 |
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| Abstract |
The E. coli low molecular mass penicillin-binding proteins (PBP's) are penicillin sensitive, enzymes involved in the terminal stages of peptidoglycan biosynthesesis. These PBP's are believed to anchor to the periplasmic face of the inner membrane via C-terminal amphiphilic alpha-helices but to date the only support for this hypothesis has been obtained from theoretical analysis. In this paper, the conformational behaviour of synthetic peptides corresponding to these C-terminal anchoring domains was studied as a function of solvent, pH, sodium dodecyl sulphate micelles and phospholipid (DOPC, DOPG) vesicles using circular dichroism (CD) spectroscopy. The CD data showed that in 2,2,2-trifluoroethanol or sodium dodecylsulphate, all three peptides have the capacity to form an alpha-helical conformation but in aqueous solution or in the presence of phospholipid vesicles only those peptides corresponding to the PBP5 and PBP6 C-termini were observed to do so. A pH dependent loss of alpha-helical conformation in the peptide corresponding to the PBP5 C-terminus was found to correlate with the susceptibility of PBP5 to membrane extraction. This correlation would agree with the hypothesis that an alpha-helical conformation is required for membrane interaction of the PBP5 C-terminal region. |
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| Keywords |
Amino Acid Sequence; Bacterial Proteins; Carrier Proteins/chemistry; Circular Dichroism; Escherichia coli; Hexosyltransferases; Liposomes; Molecular Sequence Data; Muramoylpentapeptide Carboxypeptidase/chemistry; Penicillin-Binding Proteins; Penicillins/metabolism; Peptide Fragments/chemistry; Peptides/chemical synthesis; Peptides/chemistry; Peptidyl Transferases; Phosphatidylcholines; Phosphatidylglycerols; Protein Structure, Secondary |
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