Crystal structure of penicillin-binding protein 3 (PBP3) from Escherichia coli

Eric Sauvage; Adeline Derouaux; Claudine Fraipont; Marine Joris; Raphaël Herman; Mathieu Rocaboy; Marie Schloesser; Jacques Dumas; Frédéric Kerff; Martine Nguyen-Distèche; Paulette Charlier

doi:10.1371/journal.pone.0098042

Crystal structure of penicillin-binding protein 3 (PBP3) from Escherichia coli

PLoS One. 2014 May 29;9(5):e98042. doi: 10.1371/journal.pone.0098042. eCollection 2014.

Affiliations

¹ Centre d'Ingénierie des Protéines, Université de Liège, Institut de Physique B5a et Institut de Chimie B6a, Sart Tilman, Liège, Belgium.
² Sanofi R&D, protein production, 13 quai Jules Guesde, 94403 Vitry sur Seine, France.

Abstract

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. PBP3 is mainly periplasmic, with a 23 residues cytoplasmic tail and a single transmembrane helix. 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. 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. 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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Catalytic Domain
Escherichia coli Proteins / chemistry*
Escherichia coli Proteins / genetics
Escherichia coli Proteins / isolation & purification
Escherichia coli Proteins / metabolism
Escherichia coli* / genetics
Escherichia coli* / metabolism
Models, Molecular
Penicillin-Binding Proteins / chemistry*
Penicillin-Binding Proteins / genetics
Penicillin-Binding Proteins / isolation & purification
Penicillin-Binding Proteins / metabolism
Peptidoglycan Glycosyltransferase / chemistry*
Peptidoglycan Glycosyltransferase / genetics
Peptidoglycan Glycosyltransferase / isolation & purification
Peptidoglycan Glycosyltransferase / metabolism
Protein Binding
Protein Conformation
Protein Interaction Domains and Motifs
Protein Multimerization

Substances

Escherichia coli Proteins
FtsI protein, E coli
Penicillin-Binding Proteins
Peptidoglycan Glycosyltransferase

Grants and funding

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. 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. M. J. is recipient of a FRIA (Fonds de la Recherche pour l’Industrie et l’Agriculture) fellowship (F.R.S.-FNRS, Brussels, Belgium). FK is research associates of the FRS-FNRS, Belgium. Jacques Dumas is employed by Sanofi-Aventis. 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. The specific role of this author is articulated in the ‘author contributions’ section. All other funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.