Reference : Specific Structural Features of the N-Acetylmuramoyl-l-Alanine Amidase AmiD from Escheri...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/31243
Specific Structural Features of the N-Acetylmuramoyl-l-Alanine Amidase AmiD from Escherichia coli and Mechanistic Implications for Enzymes of This Family.
English
Kerff, Frédéric mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Petrella, Stéphanie [> > > >]
Mercier, Frédéric mailto [Université de Liège - ULg > > Centre de recherches du cyclotron >]
Sauvage, Eric mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Herman, Raphaël mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Pennartz, Anne [> > > >]
Zervosen, Astrid mailto [Université de Liège - ULg > > Centre de recherches du cyclotron >]
Luxen, André mailto [Université de Liège - ULg > Département de chimie (sciences) > Chimie organique de synthèse - Centre de recherches du cyclotron >]
Frère, Jean-Marie 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 - Centre d'ingénierie des protéines >]
Charlier, Paulette mailto [Université de Liège - ULg > Département des sciences de la vie > Cristallographie des macromolécules biologiques >]
2010
Journal of Molecular Biology
Academic Press
397
249-259
Yes (verified by ORBi)
International
0022-2836
1089-8638
London
United Kingdom
[en] AmiD is the fifth identified N-acetylmuramoyl-l-alanine zinc amidase of Escherichia coli. This periplasmic lipoprotein is anchored in the outer membrane and has a broad specificity. AmiD is capable of cleaving the intact peptidoglycan (PG) as well as soluble fragments containing N-acetylmuramic acid regardless of the presence of an anhydro form or not, unlike the four other amidases, AmiA, AmiB, AmiC, and AmpD, which have some specificity. AmiD function is, however, not clearly established but it could be part of the enzymatic machinery involved in the PG turnover in E. coli. We solved three structures of the E. coli zinc amidase AmiD devoid of its lipidic anchorage: the holoenzyme, the apoenzyme in complex with the substrate anhydro-N-acetylmuramic-acid-l-Ala-gamma-d-Glu-l-Lys, and the holoenzyme in complex with the l-Ala-gamma-d-Glu-l-Lys peptide, the product of the hydrolysis of this substrate by AmiD. The AmiD structure shows a relatively flexible N-terminal extension that allows an easy reach of the PG by the enzyme inserted into the outer membrane. The C-terminal domain provides a potential extended geometrical complementarity to the substrate. AmiD shares a common fold with AmpD, the bacteriophage T7 lysozyme, and the PG recognition proteins, which are receptor proteins involved in the innate immune responses of a wide range of organisms. Analysis of the different structures reveals the similarity between the catalytic mechanism of zinc amidases of the AmiD family and the thermolysin-related zinc peptidases.
http://hdl.handle.net/2268/31243
10.1016/j.jmb.2009.12.038
Copyright (c) 2010 Elsevier Ltd. All rights reserved.

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