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3znb
From Proteopedia
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METALLO-BETA-LACTAMASE (ZN, HG-BOUND FORM)
Overview
The metallo-beta-lactamases require zinc or cadmium for hydrolyzing, beta-lactam antibiotics and are inhibited by mercurial compounds. To data, there are no clinically useful inhibitors of this class of enzymes. The, crystal structure of the Zn(2+)-bound enzyme from Bacteroides fragilis, contains a binuclear zinc center in the active site. A hydroxide, coordinated to both zinc atoms, is proposed as the moiety that mounts the, nucleophilic attack on the carbonyl carbon atom of the beta-lactam ring., To study the metal coordination further, the crystal structures of a, Cd(2+)-bound enzyme and of an Hg(2+)-soaked zinc-containing enzyme have, been determined at 2.1 A and 2.7 A, respectively. Given the diffraction, resolution, the Cd(2+)-bound enzyme exhibits the same active-site, architecture ... [(full description)]
About this Structure
3ZNB is a [Single protein] structure of sequence from [Bacteroides fragilis] with ZN, HG and NA as [ligands]. Active as [Beta-lactamase], with EC number [3.5.2.6]. Structure known Active Sites: HG, NA and ZN. Full crystallographic information is available from [OCA].
Reference
Crystal structures of the cadmium- and mercury-substituted metallo-beta-lactamase from Bacteroides fragilis., Concha NO, Rasmussen BA, Bush K, Herzberg O, Protein Sci. 1997 Dec;6(12):2671-6. PMID:9416622
Page seeded by OCA on Tue Oct 30 17:47:11 2007
Categories: Bacteroides fragilis | Beta-lactamase | Single protein | Concha, N.O. | Herzberg, O. | HG | NA | ZN | Hydrolase | Mercury | Metallo beta-lactamase | Zinc
