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Structure paper

TitleA drug-resistant beta-lactamase variant changes the conformation of its active-site proton shuttle to alter substrate specificity and inhibitor potency.
Journal, issue, pagesJ. Biol. Chem., Vol. 295, Page 18239-18255, Year 2020
Publish dateSep 9, 2020 (structure data deposition date)
AuthorsSoeung, V. / Lu, S. / Hu, L. / Judge, A. / Sankaran, B. / Prasad, B.V.V. / Palzkill, T.
External linksJ. Biol. Chem. / PubMed:33109613
MethodsX-ray diffraction
Resolution1.4 - 1.8 Å
Structure data

PDB-7k2w:
Crystal structure of CTX-M-14 E166A/K234R Beta-lactamase in complex with hydrolyzed cefotaxime
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

PDB-7k2x:
Crystal structure of CTX-M-14 E166A/K234R Beta-lactamase
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-7k2y:
Crystal structure of CTX-M-14 E166A/K234R Beta-lactamase in complex with hydrolyzed ampicillin
Method: X-RAY DIFFRACTION / Resolution: 1.62 Å

Chemicals

ChemComp-CEF:
CEFOTAXIME, C3' cleaved, open, bound form / antibiotic*YM

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

ChemComp-AIX:
(2R,4S)-2-[(1R)-1-{[(2R)-2-amino-2-phenylacetyl]amino}-2-oxoethyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid

Source
  • escherichia coli (E. coli)
KeywordsHYDROLASE / antibiotic resistance / acyl-enzyme intermediate / CTX-M-14

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