InterPro domain: IPR001279

Metallo beta lactamases exhibit low sequence identity between enzymes but they are structurally similar. They have a characteristic alpha-beta/beta-alpha sandwich fold in which the active site is at the interface between domains. Apart from the beta-lactamases and metallo-beta-lactamases, a number of other proteins contain this domain and share the same fold type [ 1 , 2 ]. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.

1. The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold. EMBO J. 14, 4914-21
2. Metallo-?-lactamase structure and function. Ann. N. Y. Acad. Sci. 1277, 91-104