Reference : NMR structure of Citrobacter freundii AmpD, comparison with bacteriophage T7 lysozyme an...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/2891
NMR structure of Citrobacter freundii AmpD, comparison with bacteriophage T7 lysozyme and homology with PGRP domains.
English
Liepinsh, Edvards [> > > >]
Genereux, Catherine mailto [Université de Liège - ULg > Département des maladies infectieuses et parasitaires > Parasitologie et pathologie des maladies parasitaires >]
Dehareng, Dominique mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines]
Joris, Bernard mailto [Université de Liège - ULg > Département des sciences de la vie > Physiologie et génétique bactériennes]
Otting, Gottfried [> > > >]
2003
Journal of Molecular Biology
Academic Press
327
4
833-42
Yes
International
0022-2836
1089-8638
London
United Kingdom
[en] Amino Acid Sequence ; zinc amidase ; peptidoglycan recognition protein domain ; NMR structure ; beta-lactamase induction ; AmpD ; Bacterial Proteins/chemistry/genetics/isolation & purification ; Bacteriophage T7/enzymology ; Carrier Proteins/chemistry ; Citrobacter freundii/chemistry ; Conserved Sequence ; Escherichia coli/genetics ; Eukaryotic Cells/chemistry ; Magnetic Resonance Spectroscopy ; Models, Chemical ; Models, Molecular ; Molecular Sequence Data ; Mutation ; N-Acetylmuramoyl-L-alanine Amidase/chemistry/genetics/isolation & purification ; Protein Conformation ; Sequence Homology, Amino Acid ; Species Specificity ; Substrate Specificity ; Zinc/analysis
[en] AmpD is a bacterial amidase involved in the recycling of cell-wall fragments in Gram-negative bacteria. Inactivation of AmpD leads to derepression of beta-lactamase expression, presenting a major pathway for the acquisition of constitutive antibiotic resistance. Here, we report the NMR structure of AmpD from Citrobacter freundii (PDB accession code 1J3G). A deep substrate-binding pocket explains the observed specificity for low molecular mass substrates. The fold is related to that of bacteriophage T7 lysozyme. Both proteins bind zinc at a conserved site and require zinc for amidase activity, although the enzymatic mechanism seems to differ in detail. The structure-based sequence alignment identifies conserved features that are also conserved in the eukaryotic peptidoglycan recognition protein (PGRP) domains, including the zinc-coordination site in several of them. PGRP domains thus belong to the same fold family and, where zinc-binding residues are conserved, may have amidase activity. This hypothesis is supported by the observation that human serum N-acetylmuramyl-L-alanine amidase seems to be identical with a soluble form of human PGRP-L.
Research School of Chemistry Australian National University Canberra ; Center for Protein Engineering, Liege University ; Department of Medical Biochemistry and Biophysics Karolinska Institute, Stockholm
Politique Scientifique Fédérale (Belgique) = Belgian Federal Science Policy ; Swedish NMR Centre ; Swedish Council ; Fonds pour la formation à la Recherche dans l'Industrie et dans l'Agriculture (Communauté française de Belgique) - FRIA ; Fonds de la Recherche Scientifique (Communauté française de Belgique) - F.R.S.-FNRS
Researchers ; Students ; Professionals
http://hdl.handle.net/2268/2891
also: http://hdl.handle.net/2268/125368
10.1016/S0022-2836(03)00185-2
Copyright 2003 Published by Elsevier Science Ltd.

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