| 词条 | Metallo-beta-lactamase protein fold |
| 释义 |
| Symbol = Lactamase_B | Name = Metallo-beta-lactamase superfamily | image = 1BMC.png | width = | caption = 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.[1] | Pfam = PF00753 | InterPro = IPR001279 | SMART = | PROSITE = | SCOP = 1bmc | TCDB = | OPM family = | OPM protein = | PDB = {{PDB2|1a7t}}, {{PDB2|1a8t}}, {{PDB2|1bc2}}, {{PDB2|1bmc}}, {{PDB2|1bvt}}, {{PDB2|1dd6}}, {{PDB2|1ddk}}, {{PDB2|1dxk}}, {{PDB2|1e5d}}, {{PDB2|1hlk}}, {{PDB2|1jjt}}, {{PDB2|1jt1}}, {{PDB2|1k07}}, {{PDB2|1ko2}}, {{PDB2|1ko3}}, {{PDB2|1kr3}}, {{PDB2|1l9y}}, {{PDB2|1m2x}}, {{PDB2|1mqo}}, {{PDB2|1p9e}}, {{PDB2|1qh3}}, {{PDB2|1qh5}}, {{PDB2|1sml}}, {{PDB2|1vgn}}, {{PDB2|1vme}}, {{PDB2|1wuo}}, {{PDB2|1wup}}, {{PDB2|1ww1}}, {{PDB2|1x8g}}, {{PDB2|1x8h}}, {{PDB2|1x8i}}, {{PDB2|1xm8}}, {{PDB2|1y44}}, {{PDB2|1ycf}}, {{PDB2|1ycg}}, {{PDB2|1ych}}, {{PDB2|1znb}}, {{PDB2|2aio}}, {{PDB2|2bc2}}, {{PDB2|2bfz}}, {{PDB2|2bg2}}, {{PDB2|2bg6}}, {{PDB2|2bg7}}, {{PDB2|2bg8}}, {{PDB2|2bga}}, {{PDB2|2bmi}}, {{PDB2|2cbn}}, {{PDB2|2fk6}}, {{PDB2|2znb}}, {{PDB2|3bc2}}, {{PDB2|3znb}}, {{PDB2|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] See also
References1. ^1 {{PDB|1bmc}} ; {{cite journal |vauthors=Carfi A, Pares S, Duée E, Galleni M, Duez C, Frère JM, Dideberg O | title = The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold | journal = EMBO J. | volume = 14 | issue = 20 | pages = 4914–21 |date=October 1995 | pmid = 7588620 | pmc = 394593 | doi = 10.1002/j.1460-2075.1995.tb00174.x| url = }} {{InterPro content|IPR001279}}2. ^{{cite web| title = Inhibition of metallo-β-lactamase| id = 7456274| author = Shaw, Robert W| author2 = Kim, Sung-kun| date = November 2008 | url = http://www.freepatentsonline.com/7456274.html}} 3. ^{{cite journal |vauthors=Alderson R, Barker D, Mitchell JB |title=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 |journal=J. Mol. Evol. |year=2014 |pmid=25185655 |doi=10.1007/s00239-014-9639-7 |volume=79 |issue=3–4 |pages=117–29 |pmc=4185109}} 3 : Protein domains|Protein superfamilies|Protein folds |
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