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Crystal structure of penicillin-binding protein 3 (PBP3) from Escherichia coli.
Sauvage E, Derouaux A, Fraipont C, Joris M, Herman R, Rocaboy M, Schloesser M, Dumas J, Kerff F, Nguyen-Distèche M, Charlier P. Sauvage E, et al. Among authors: fraipont c. PLoS One. 2014 May 29;9(5):e98042. doi: 10.1371/journal.pone.0098042. eCollection 2014. PLoS One. 2014. PMID: 24875494 Free PMC article.
Functional analysis of the cell division protein FtsW of Escherichia coli.
Pastoret S, Fraipont C, den Blaauwen T, Wolf B, Aarsman ME, Piette A, Thomas A, Brasseur R, Nguyen-Distèche M. Pastoret S, et al. Among authors: fraipont c. J Bacteriol. 2004 Dec;186(24):8370-9. doi: 10.1128/JB.186.24.8370-8379.2004. J Bacteriol. 2004. PMID: 15576787 Free PMC article.
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. Among authors: fraipont c. 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.
21 results