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
|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.|
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.
 See also
- 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. //www.ncbi.nlm.nih.gov/pmc/articles/PMC394593/.
- "Shaw, Robert W. (Lubbock, TX, US), Kim, Sung-kun (Lubbock, TX, US)" ("November" "2008"). "Inhibition of metallo-β-lactamase". http://www.freepatentsonline.com/7456274.html.
Metallo-beta-lactamase superfamily Provide feedback
No Pfam abstract.
Carfi A, Pares S, Duee E, Galleni M, Duez C, Frere JM, Dideberg O; , EMBO J 1995;14:4914-4921.: The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold. PUBMED:7588620 EPMC:7588620
Internal database links
|Similarity to PfamA using HHSearch:||Lactamase_B_2 Lactamase_B_3 Lactamase_B_4|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR001279Apart from the beta-lactamases and metallo-beta-lactamases, a number of other proteins contain this domain [PUBMED:7588620]. 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.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||hydrolase activity (GO:0016787)|
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Curation and family details
|Author:||Ponting CP, Bateman A|
|Number in seed:||305|
|Number in full:||34807|
|Average length of the domain:||193.00 aa|
|Average identity of full alignment:||14 %|
|Average coverage of the sequence by the domain:||50.57 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||22|
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There are 5 interactions for this family. More...
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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 domain has been found. There are 350 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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