Protein Family Models

The penicillin-binding proteins are bifunctional proteins consisting of transglycosylase and transpeptidase in the N- and C-terminus respectively [1]. The transglycosylase domain catalyses the polymerisation of murein glycan chains ([4]). [1]. 9244263. Topographical and functional investigation of Escherichia coli penicillin-binding protein 1b by alanine stretch scanning mutagenesis. F. Lefevre, M. H. Remy & J. M. Masson;. J Bacteriol 1997;179:4761-4767. [2]. 9614972. X-ray studies of enzymes that interact with penicillins. Kelly JA, Kuzin AP, Charlier P, Fonze E;. Cell Mol Life Sci 1998;54:353-358. [3]. 8830253. Monofunctional biosynthetic peptidoglycan transglycosylases. Spratt BG, Zhou J, Taylor M, Merrick MJ;. Mol Microbiol 1996;19:639-640. [4]. 12867450. The glycosyltransferase domain of penicillin-binding protein 2a from Streptococcus pneumoniae catalyzes the polymerization of murein glycan chains. Di Guilmi AM, Dessen A, Dideberg O, Vernet T;. J Bacteriol 2003;185:4418-4423. (from Pfam)

Date:

2024-10-16

The active site serine (residue 337 in Swiss:P14677) is conserved in all members of this family. [1]. 8605631. X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin target enzyme. Pares S, Mouz N, Petillot Y, Hakenbeck R, Dideberg O. Nat Struct Biol 1996;3:284-289. (from Pfam)

Date:

2024-10-16

penicillin-binding protein 1A is a bifunctional transpeptidases/transglycosylase that catalyzes synthesis of cross-linked peptidoglycan from the lipid intermediates in cell wall formation

Date:

2024-09-03