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Structure paper

TitleKPC-2 beta-lactamase enables carbapenem antibiotic resistance through fast deacylation of the covalent intermediate.
Journal, issue, pagesJ. Biol. Chem., Vol. 296, Page 100155-100155, Year 2020
Publish dateJun 10, 2020 (structure data deposition date)
AuthorsMehta, S.C. / Furey, I.M. / Pemberton, O.A. / Boragine, D.M. / Chen, Y. / Palzkill, T.
External linksJ. Biol. Chem. / PubMed:33273017
MethodsX-ray diffraction
Resolution1.2 - 2.05 Å
Structure data

PDB-6xd5:
Apo KPC-2 N170A mutant at 1.20 A
Method: X-RAY DIFFRACTION / Resolution: 1.2 Å

PDB-6xd7:
KPC-2 N170A mutant bound to hydrolyzed ampicillin at 1.65 A
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

PDB-6xj8:
KPC-2 N170A mutant bound to hydrolyzed imipenem at 2.05 A
Method: X-RAY DIFFRACTION / Resolution: 2.05 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-ZZ7:
(2R,4S)-2-[(R)-{[(2R)-2-amino-2-phenylacetyl]amino}(carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid

ChemComp-8YF:
(2R)-2-[(2S,3R)-1,3-bis(oxidanyl)-1-oxidanylidene-butan-2-yl]-4-(2-methanimidamidoethylsulfanyl)-2,3-dihydro-1H-pyrrole / antibiotic*YM

Source
  • klebsiella pneumoniae (bacteria)
KeywordsHYDROLASE / carbapenemase / beta-lactamase / HYDROLASE/Antibiotic / antibiotic / HYDROLASE-Antibiotic complex / antibiotic complex

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