Metallo-beta-lactamase protein fold
The metallo-beta-lactamase protein fold is a protein domain contained in class B beta-lactamases and a number of other proteins . 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.
Metallo-beta-lactamases are important enzymes because they are involved in the breakdown of antibiotics by antibiotic-resistant bacteria. It is unclear whether metallo-beta-lactamse activity evolved once or twice within the superfamily; if twice, this would suggest structural exaptation.
- PDB 1bmc ; Carfi A, Pares S, Duée E, Galleni M, Duez C, Frère JM, Dideberg O (October 1995). "The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold". EMBO J. 14 (20): 4914–21. PMC 394593. PMID 7588620.
- "Shaw, Robert W. (Lubbock, TX, US), Kim, Sung-kun (Lubbock, TX, US)" ("November" "2008"). "Inhibition of metallo-β-lactamase" ("7456274"). Check date values in:
- Alderson R, Barker D, Mitchell JBO (2014). "One origin for metallo-beta-lactamase activity, or two? An investigation assessing a diverse set of reconstructed ancestral sequences based on a sample of phylogenetic trees". J. Mol. Evol. doi:10.1007/s00239-014-9639-7. PMID 25185655.