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Publication Abstract from PubMed

In Escherichia coli, penicillin-binding protein 3 (PBP3), also known as FtsI, is a central component of the divisome, catalyzing cross-linking of the cell wall peptidoglycan during cell division. PBP3 is mainly periplasmic, with a 23 residues cytoplasmic tail and a single transmembrane helix. We have solved the crystal structure of a soluble form of PBP3 (PBP357-577) at 2.5 A revealing the two modules of high molecular weight class B PBPs, a carboxy terminal module exhibiting transpeptidase activity and an amino terminal module of unknown function. To gain additional insight, the PBP3 Val88-Ser165 subdomain (PBP388-165), for which the electron density is poorly defined in the PBP3 crystal, was produced and its structure solved by SAD phasing at 2.1 A. The structure shows a three dimensional domain swapping with a beta-strand of one molecule inserted between two strands of the paired molecule, suggesting a possible role in PBP357-577 dimerization.

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-Disteche M, Charlier P PLoS One. 2014 May 29;9(5):e98042. doi: 10.1371/journal.pone.0098042. eCollection, 2014. PMID:24875494^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.