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The former enzymes act as transpeptidases in vivo and are involved in peptidoglycan synthesis while the latter are carboxypeptidases and endopeptidases thought to remodel peptidoglycan during the bacterial life cycle but details of their in vivo activities are not well established. Penicillin-binding proteins belong to the family of acyl-serine transferases and are traditionally separated into high-molecular-weight (HMW) PBPs and low-molecular-weight (LMW) PBPs based on molecular weight and sequence homology –. They are found in all bacteria and represent major targets in anti-biotherapy, especially for the widely used β-lactam antibiotics. The penicillin-binding proteins (PBPs) synthesize and remodel the cell wall peptidoglycan, a major component of the bacterial cell wall that gives the cell its shape and rigidity –. This does not alter the authors’ adherence to PLOS ONE policies on sharing data and materials. All other funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.Ĭompeting interests: Jacques Dumas is employed by Sanofi-Aventis. The specific role of this author is articulated in the ‘author contributions’ section. Sanofi-Aventis provided support in the form of salary for author JD, but did not have any additional role in the study design, data collection and analysis, decision to publish, or preparation of the manuscript. Jacques Dumas is employed by Sanofi-Aventis. FK is research associates of the FRS-FNRS, Belgium. is recipient of a FRIA (Fonds de la Recherche pour l’Industrie et l’Agriculture) fellowship (F.R.S.-FNRS, Brussels, Belgium). P6/19), the Fonds de la Recherche Scientifique, (IISN 4.4505.09, IISN 4.4509.11, FRFC 2.4511.06F), the University of Liège (Fonds spéciaux, Crédit classique, C-06/19 and C-09/75), and a return grant to AD.
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This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.įunding: This work was supported in part by the Belgian Program on Interuniversity Poles of Attraction initiated by the Belgian State, Prime Minister’s Office, Science Policy programming (IAP no. Received: JanuAccepted: ApPublished: May 29, 2014Ĭopyright: © 2014 Sauvage et al.
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PLoS ONE 9(5):Įditor: Eric Cascales, Centre National de la Recherche Scientifique, Aix-Marseille Université, France (2014) Crystal Structure of Penicillin-Binding Protein 3 (PBP3) from Escherichia coli. 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.Citation: Sauvage E, Derouaux A, Fraipont C, Joris M, Herman R, Rocaboy M, et al. 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.
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Staphylococcus aureus is a widespread Gram-positive opportunistic pathogen, and a methicillin-resistant form (MRSA) is particularly difficult to treat clinically.