Metallo-beta-lactamase protein fold

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Metallo-beta-lactamase superfamily
1BMC.png
Cartoon diagram of the crystallographic structure of a zinc metallo-beta-lactamase from bacillus cereus (N-terminus = blue, C-terminus = blue) The catalytic zinc ion is depicted as a grey sphere.[1]
Identifiers
Symbol Lactamase_B
Pfam PF00753
InterPro IPR001279
SCOP 1bmc
SUPERFAMILY 1bmc

The metallo-beta-lactamase protein fold is a protein domain contained in class B beta-lactamases and a number of other proteins .[1] 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.[2]

See also[edit]

References[edit]

  1. ^ a b 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. 
  2. ^ "Shaw, Robert W. (Lubbock, TX, US), Kim, Sung-kun (Lubbock, TX, US)" ("November" "2008"). "Inhibition of metallo-β-lactamase" ("7456274"). 

This article incorporates text from the public domain Pfam and InterPro IPR001279