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. the class B PBP3 possibly involved in intra- and intermolecular interactions, the mean -helical hydrophobic moment and the mean hydrophobicity were calculated along the amino acid sequence of the protein. 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. 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. 351-364 ISSN: 0022-2836 Subject: Staphylococcus aureus, cefotaxime, crystal structure, dimerization, mass spectrometry, models, pathogens, ultracentrifugation Abstract: Staphylococcus aureus is a widespread Gram‐positive opportunistic pathogen, and a methicillin‐resistant form (MRSA) is particularly difficult to treat clinically. It consists of a short intracellular M1-R23 peptide fused to an F24-元9 membrane anchor that is linked via a G40-S70 peptide to an R71-I236 noncatalytic module, itself linked to a D237-V577 catalytic penicillin-binding module. Tame, Sam-Yong Park Source: Journal of molecular biology 2012 v.423 no.3 pp. The multimodular class B PBP3 specifically catalyzes peptide cross-bridges of the septal cell wall peptidoglycan during cell division. 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.Crystal Structures of Penicillin-Binding Protein 3 (PBP3) from Methicillin-Resistant Staphylococcus aureus in the Apo and Cefotaxime‐Bound Forms Author: Hisashi Yoshida, Fumihiro Kawai, Eiji Obayashi, Satoko Akashi, David I. 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.
Low-molecular-weight class C PBPs, including PBP4 and PBP5, are soluble pro-teins andact asDD carboxypeptidases. High-molecular-weight class B PBP, of which Pseudomonas PBP3 is a member, possesses only transpeptidase activity. 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. class A PBPs (PBP1a and PBP1b) are bifunctional enzymes con-taining both transglycosylase and transpeptidase activities.
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. Seven PBP genes and one monofunctional transglycosylase (MGT) gene were identified in the six genomes, encoding (i) four high-molecular-mass proteins (two of class A, PBP1a ponA and PBP1b mrcB, and two of class B, PBP2 pbpA or mrdA and PBP3 ftsI), (ii) three low-molecular-mass proteins (two of type 5, PBP5/6 dacC and PBP6b dacD, and one of type 7 (PBP7/8 pbpG), and (iii) a.
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. Staphylococcus aureus is a widespread Gram-positive opportunistic pathogen, and a methicillin-resistant form (MRSA) is particularly difficult to treat clinically.