[en] The metallo--lactamase superfamily comprises a remarkable set of enzymes that catalyse the hydrolysis of a wide range of substrates such as peptides, nucleic acids, antibiotics of the penicillin family and organophosphorus derivatives. In the past ten years, X-Ray structures of representative enzymes from different families have been determined, with the metallo--lactamases being the most represented. The salient common structural feature is the presence of a catalytic metal centre embedded within a fold. The wealth of sequence and structural information on metallo--lactamases has allowed their classification into three subclasses. Structural information is now available for members of each subclass. Interestingly, these structures show the presence of either a mono or a di-nuclear metal centre in the active sites raising questions on the metal to protein stoichiometry under physiological conditions. In addition, the structures reveal a wide variability in the shape of the active site, which involves three variable loops lining the metal centre. For each enzyme a clear correlation is found between active site shape and substrate specificity.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Bebrone, Carine ; Université de Liège - ULiège > Centre d'Ingénierie des Protéines
Garau, Gianpiero; Institut de Biologie Structurale Jean-Pierre Ebel
Garcia-Saez, Isabel; Institut de Biologie Structurale Jean-Pierre Ebel