ORBi: Dideberg O. - Structure of a Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase at 2.5 A resolution.

Reference : Structure of a Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase at 2.5 A res...


	Document type :	Scientific journals : Article
	Discipline(s) :	Life sciences : Biochemistry, biophysics & molecular biology
	To cite this reference:	http://hdl.handle.net/2268/77995

Title :	Structure of a Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase at 2.5 A resolution.
Language :	English
Author, co-author :	Dideberg, O. [Université de Liège - ULg > > Laboratoire de Cristallographie > >]
	Charlier, Paulette [Université de Liège - ULg > Département des sciences de la vie > Cristallographie des macromolécules biologiques >]
	Dive, Georges [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
	Joris, Bernard [Université de Liège - ULg > Département des sciences de la vie > Physiologie et génétique bactériennes - Centre d'ingénierie des protéines >]
	Frère, Jean-Marie [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
	Ghuysen, Jean-Marie [Université de Liège - ULg > > > > Centre d'ingénierie des protéines > >]
Publication date :	1982
Journal title :	Nature
Publisher :	Nature Publishing Group
Volume :	299
Issue/season :	5882
Pages :	469-470
Audience :	International
ISSN :	0028-0836
e-ISSN :	1476-4687
City :	Basingstoke
Country :	United Kingdom
Keywords :	[en] Carboxypeptidases/metabolism ; Catalysis ; Metalloproteins ; Muramoylpentapeptide Carboxypeptidase/metabolism ; Protein Conformation ; Streptomyces/enzymology ; X-Ray Diffraction ; Zinc
Abstract :	[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.
Permalink :	http://hdl.handle.net/2268/77995
DOI :	10.1038/299469a0

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