Abstract
Bacteria possess proteases that are specific for the peptide bonds between D-alanine residues, one of which has a free α-carboxyl group. These D-alanyl-D-alanine peptidases catalyse carboxypeptidation and transpeptidation reactions involved in bacterial cell wall metabolism1,2, and are inactivated by β-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 α-helices, and the C-terminal domain has three α-helices and five β-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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Dideberg, O., Charlier, P., Dive, G. et al. Structure of a Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase at 2.5 Å resolution. Nature 299, 469–470 (1982). https://doi.org/10.1038/299469a0
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DOI: https://doi.org/10.1038/299469a0
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