Summary: Metallo-beta-lactamase superfamily
This is the Wikipedia entry entitled "Metallo-beta-lactamase protein fold". More...
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Metallo-beta-lactamase protein fold Edit Wikipedia article
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-lactamase activity evolved once or twice within the superfamily; if twice, this would suggest structural exaptation.
- "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. ; Carfi A, Pares S, Duée E, Galleni M, Duez C, Frère JM, Dideberg O (October 1995).
- "Shaw, Robert W. (Lubbock, TX, US), Kim, Sung-kun (Lubbock, TX, US)" ("2008"). "Inhibition of metallo-β-lactamase" ("7456274"). Unknown parameter
|date=suggested) (help); 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. 79: 117–29. doi:10.1007/s00239-014-9639-7. PMID 25185655.
Metallo-beta-lactamase superfamily Provide feedback
This is a small family of putative metal-dependent hydrolases.
External database links
This tab holds annotation information from the InterPro database.
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This example describes an architecture with one
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This superfamily of enzymes including beta-lactamases, thiolesterases, members of the glyoxalase II family that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid all bind two ions of zinc. An additional family of competence proteins essential for natural transformation do not appear to bind zinc, and might be a transporter involved in DNA uptake.
The clan contains the following 8 members:Beta_lactamase3 Lactamase_B Lactamase_B_2 Lactamase_B_3 Lactamase_B_4 Lactamase_B_5 Lactamase_B_6 PDEase_II
We make a range of alignments for each Pfam-A family:
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Curation and family details
|Number in seed:||4|
|Number in full:||29|
|Average length of the domain:||194.20 aa|
|Average identity of full alignment:||42 %|
|Average coverage of the sequence by the domain:||88.35 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||2|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Lactamase_B_5 domain has been found. There are 2 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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