The structure shows a three dimensional domain swapping with a β-strand of one molecule inserted between two strands of the paired molecule, suggesting a possible role in PBP3(57-577) dimerization.Ĭentre d'Ingénierie des Protéines, Université de Liège, Institut de Physique B5a et Institut de Chimie B6a, Sart Tilman, Liège, Belgium. To gain additional insight, the PBP3 Val88-Ser165 subdomain (PBP3(88-165)), for which the electron density is poorly defined in the PBP3 crystal, was produced and its structure solved by SAD phasing at 2.1 Å. We have solved the crystal structure of a soluble form of PBP3 (PBP3(57-577)) at 2.5 Å 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. identified a PBP3 homolog in Salmonella Typhimurium that is preferentially involved in septation at low pH (Castanheira et al., 2017). coli carboxypeptidase PBP6b plays a key role in maintenance of cell morphology during growth at pH 5.0 (Peters et al., 2016b), while Castanheira et al. PBP3 is mainly periplasmic, with a 23 residues cytoplasmic tail and a single transmembrane helix. Peters and colleagues demonstrated that E. Read more about user accounts at EcoliWiki membership.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. coli targets click here.ĮcoliWiki members can use EcoliWiki in ways that are not available to unregistered users. Tell us what you want to see on EcoliWikiĮcoliWiki participates in the RefGenome project.Add new pages about topics you're interested in.There are lots of ways you can help us make EcoliWiki better: Identity and Function of a Large Gene Network Underlying Mutagenic Repair of DNA BreaksĮcoliWiki is for everyone. Some sample queries are listed below, and you can always read more about searching on our Help pages.

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Pbp3 e.coli