FtsI (penicillin-binding protein 3, PBP3) is an essential cell division protein Spratt75 which.
![pbp3 dimer pbp3 dimer](https://files.rcsb.org/pub/pdb/validation_reports/vs/3vsk/3vsk_multipercentile_validation.png)
In doing so, it varies the substrates for transpeptidation and plays a key role in maintaining cell shape. Reaction, 2 a peptidoglycan dimer (meso-diaminopimelate. This dimer form is predicted to be highly stable in solution by the PISA server, but mass spectrometry and analytical ultracentrifugation provide unequivocal evidence that the protein is a monomer in solution. Penicillin-binding protein 5 (PBP5) is a dd-carboxypeptidase, which cleaves the terminal d-alanine from the muramyl pentapeptide in the peptidoglycan layer of Escherichia coli and other bacteria. We have solved the crystal structure of a soluble. PBP3 is mainly periplasmic, with a 23 residues cytoplasmic tail and a single transmembrane helix. aureus) a peptidoglycan with D,D cross-link (S. faeciums) + H + a peptidoglycan tetramer with a D,D cross-link (Enterococcus faecium) + D-alanine 2 a peptidoglycan dimer (S. In vitro murein peptidoglycan synthesis by dimers of. 2 a peptidoglycan dimer (meso-diaminopimelate containing) periplasm a peptidoglycan with D,D cross-links (meso-diaminopimelate containing) periplasm + D-alanine periplasm2 a peptidoglycan dimer (E. Consistent with the nomenclature of “dimerization domain”, the N-terminal region forms an apparently tight interaction with a neighboring molecule related by a 2-fold symmetry axis in the crystal structure. 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. The implications of this substrate specificity of NG PBP3 with respect to its. The model shows a different orientation of its two domains compared to earlier models of other class B PBPs and a novel, larger N-domain. PBP3 is a class B PBP, possessing an N-terminal non-penicillin‐binding domain, sometimes called a dimerization domain, and a C-terminal transpeptidase domain. We have solved two crystal structures of penicillin‐binding protein (PBP) 3 (PBP3) from MRSA, the apo form and a complex with the β-lactam antibiotic cefotaxime, and used electrospray mass spectrometry to measure its sensitivity to a variety of penicillin derivatives.
![pbp3 dimer pbp3 dimer](https://royalsocietypublishing.org/cms/asset/3f909873-69d0-4994-ad93-3b55ab8e598a/rstb20150031f01.jpg)
Staphylococcus aureus is a widespread Gram‐positive opportunistic pathogen, and a methicillin‐resistant form (MRSA) is particularly difficult to treat clinically.