Metallo-beta-lactamase protein fold

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary
PDB	1a7t, 1a8t, 1bc2, 1bmc, 1bvt, 1dd6, 1ddk, 1dxk, 1e5d, 1hlk, 1jjt, 1jt1, 1k07, 1ko2, 1ko3, 1kr3, 1l9y, 1m2x, 1mqo, 1p9e, 1qh3, 1qh5, 1sml, 1vgn, 1vme, 1wuo, 1wup, 1ww1, 1x8g, 1x8h, 1x8i, 1xm8, 1y44, 1ycf, 1ycg, 1ych, 1znb, 2aio, 2bc2, 2bfz, 2bg2, 2bg6, 2bg7, 2bg8, 2bga, 2bmi, 2cbn, 2fk6, 2znb, 3bc2, 3znb, 4znb

Metallo-beta-lactamase superfamily
Metallo-beta-lactamase superfamily
	Cartoon diagram of the crystallographic structure of a zinc metallo-beta-lactamase from bacillus cereus (N-terminus = blue, C-terminus = red) The catalytic zinc ion is depicted as a grey sphere.
Identifiers
Symbol	Lactamase_B
Pfam	PF00753
InterPro	IPR001279
SCOP2	1bmc / SCOPe / SUPFAM
Pfam
Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary
PDB	1a7t, 1a8t, 1bc2, 1bmc, 1bvt, 1dd6, 1ddk, 1dxk, 1e5d, 1hlk, 1jjt, 1jt1, 1k07, 1ko2, 1ko3, 1kr3, 1l9y, 1m2x, 1mqo, 1p9e, 1qh3, 1qh5, 1sml, 1vgn, 1vme, 1wuo, 1wup, 1ww1, 1x8g, 1x8h, 1x8i, 1xm8, 1y44, 1ycf, 1ycg, 1ych, 1znb, 2aio, 2bc2, 2bfz, 2bg2, 2bg6, 2bg7, 2bg8, 2bga, 2bmi, 2cbn, 2fk6, 2znb, 3bc2, 3znb, 4znb

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] It is unclear whether metallo-beta-lactamase activity evolved once or twice within the superfamily; if twice, this would suggest structural exaptation.^[3]

References

^ ^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.
^ Shaw, Robert W; Kim, Sung-kun (November 2008). "Inhibition of metallo-β-lactamase". 7456274.
^ Alderson R, Barker D, Mitchell JB (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. 79: 117–29. doi:10.1007/s00239-014-9639-7. PMC 4185109. PMID 25185655.

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

[pmid7588620-1] 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; Kim, Sung-kun (November 2008). "Inhibition of metallo-β-lactamase". 7456274.

[3] Alderson R, Barker D, Mitchell JB (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. 79: 117–29. doi:10.1007/s00239-014-9639-7. PMC 4185109. PMID 25185655.

[1]

[2]

[3]

See also

References