Reference : Crystal structure of the Bacillus subtilis penicillin-binding protein 4a, and its com...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/5996
Crystal structure of the Bacillus subtilis penicillin-binding protein 4a, and its complex with a peptidoglycan mimetic peptide
English
Sauvage, Eric mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Duez, Colette mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Herman, Raphaël mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Kerff, Frédéric mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Petrella, Stéphanie [Université Pierre et Marie Curie, Paris France > > > > Lab. Recherche Moléculaire sur les Antibiotiques INSERM U655 > >]
Anderson, John W. [>Wesleyan University, CT USA > > >Department of Chemistry > > >]
Adediran, Suara A. [>Wesleyan University, CT USA > > >Department of Chemistry > > >]
Pratt, Rex F. [Wesleyan University, CT USA > > >Department of Chemistry > > >]
Frère, Jean-Marie mailto [Université de Liège - ULg > Département des sciences de la vie > Département des sciences de la vie >]
Charlier, Paulette mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
10-Aug-2007
Journal of Molecular Biology
Academic Press Ltd Elsevier Science Ltd
371
2
528-539
Yes (verified by ORBi)
International
0022-2836
London
UK
[en] penicillin-binding protein ; DD-peptidases ; Bacillus subtilis ; peptidoglycan ; diaminopimelic acid
[en] The genome of Bacillus subtilis encodes 16 penicillin-binding proteins (PBPs) involved in the synthesis and/or remodelling of the peptidoglycan during the complex life cycle of this sporulating Gram-positive rod-shaped bacterium. PBP4a (encoded by the dacC gene) is a low-molecular mass PBP clearly exhibiting in vitro DD-carboxypeptidase activity. We have solved the crystal structure of this protein alone and in complex with a peptide (D-alpha'-aminopymelyl-epsilon-D-alanyl-D-alanine) that mimics the C-terminal end of the Bacillus peptidoglycan stem peptide. PBP4a is composed of three domains: the penicillin-binding domain with a fold similar to the class A 13-lactamase structure and two domains inserted between the conserved motifs 1 and 2 characteristic of the penicillin-recognizing enzymes. The soaking of PBP4a in a solution Of D-alpha-aminopymelyl-epsilon-D-alanyl-D-alanine resulted in an adduct between PBP4a and a D-alpha-aminopimelyl-epsilon-D-alanine dipeptide and an unbound D-alanine, i.e. the products of acylation of PBP4a by D-alpha-aminopymelyl-epsilon-D-alanyl-D-alanine with the release of a D-alanine. The adduct also reveals a binding pocket specific to the diaminopimelic acid, the third residue of the peptidoglycan stem pentapeptide of B. subtilis. This pocket is specific for this class of PBPs. (C) 2007 Elsevier Ltd. All rights reserved.
http://hdl.handle.net/2268/5996
10.1016/j.jmb.2007.05.071

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