Reference : Structure of a Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase at 2.5 A ...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
Structure of a Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase at 2.5 A resolution.
Dideberg, O. [Université de Liège - ULg > > Laboratoire de Cristallographie > >]
Charlier, Paulette mailto [Université de Liège - ULg > Département des sciences de la vie > Cristallographie des macromolécules biologiques >]
Dive, Georges [Université de Liège - ULg > > >]
Joris, Bernard mailto [Université de Liège - ULg > Département des sciences de la vie > Physiologie et génétique bactériennes >]
Frère, Jean-Marie mailto [Université de Liège - ULg > > >]
Ghuysen, Jean-Marie [Université de Liège - ULg > > >]
Nature Publishing Group
Yes (verified by ORBi)
United Kingdom
[en] Carboxypeptidases/metabolism ; Catalysis ; Metalloproteins ; Muramoylpentapeptide Carboxypeptidase/metabolism ; Protein Conformation ; Streptomyces/enzymology ; X-Ray Diffraction ; Zinc
[en] Bacteria possess proteases that are specific for the peptide bonds between D-alanine residues, one of which has a free alpha-carboxyl group. These D-alanyl-D-alanine peptidases catalyse carboxypeptidation and transpeptidation reactions involved in bacterial cell wall metabolism1,2, and are inactivated by beta-lactam antibiotics. We have now elucidated the structure, at 2.5 Å resolution, of the penicillin-resistant Zn2+-containing D-alanyl-D-alanine peptidase of Streptomyces albus (Zn2+ G peptidase)3,4. The enzyme is shown to consist of two globular domains, connected by a single link. The N-terminal domain has three alpha-helices, and the C-terminal domain has three alpha-helices and five beta-strands. The Zn2+ ion is ligated by three histidine residues, and located in a cleft in the C-terminal domain. The mechanism of action of the enzyme may be related to that of other carboxypeptidases, which also contain functional Zn2+ ions.

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