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The non-penicillin-binding module of the tripartite penicillin-binding protein 3 of Escherichia coli is required for folding and/or stability of the penicillin-binding module and the membrane-anchoring module confers cell septation activity on the folded structure.
Goffin C, Fraipont C, Ayala J, Terrak M, Nguyen-Distèche M, Ghuysen JM. Goffin C, et al. J Bacteriol. 1996 Sep;178(18):5402-9. doi: 10.1128/jb.178.18.5402-5409.1996. J Bacteriol. 1996. PMID: 8808928 Free PMC article.
The bimodular G57-V577 polypeptide chain of the class B penicillin-binding protein 3 of Escherichia coli catalyzes peptide bond formation from thiolesters and does not catalyze glycan chain polymerization from the lipid II intermediate.
Adam M, Fraipont C, Rhazi N, Nguyen-Distèche M, Lakaye B, Frère JM, Devreese B, Van Beeumen J, van Heijenoort Y, van Heijenoort J, Ghuysen JM. Adam M, et al. J Bacteriol. 1997 Oct;179(19):6005-9. doi: 10.1128/jb.179.19.6005-6009.1997. J Bacteriol. 1997. PMID: 9324244 Free PMC article.
57 results