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TitleSynergistic effects of functionally distinct substitutions in beta-lactamase variants shed light on the evolution of bacterial drug resistance.
Journal, issue, pagesJ. Biol. Chem., Vol. 293, Page 17971-17984, Year 2018
Publish dateApr 6, 2018 (structure data deposition date)
AuthorsPatel, M.P. / Hu, L. / Brown, C.A. / Sun, Z. / Adamski, C.J. / Stojanoski, V. / Sankaran, B. / Prasad, B.V.V. / Palzkill, T.
External linksJ. Biol. Chem. / PubMed:30275013
MethodsX-ray diffraction
Resolution1.6 - 1.82 Å
Structure data

PDB-6cyk:
CTX-M-14 N106S mutant
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-6cyn:
CTX-M-14 N106S/D240G mutant
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-6cyq:
Crystal structure of CTX-M-14 S70G/N106S beta-lactamase in complex with hydrolyzed cefotaxime
Method: X-RAY DIFFRACTION / Resolution: 1.698 Å

PDB-6cyu:
Crystal structure of CTX-M-14 S70G/N106S/D240G beta-lactamase in complex with hydrolyzed cefotaxime
Method: X-RAY DIFFRACTION / Resolution: 1.82 Å

Chemicals

ChemComp-ACT:
ACETATE ION

ChemComp-HOH:
WATER

ChemComp-CE4:
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino}(carboxy)methyl]-5-methylidene-5,6-dihydro / antibiotic*YM

ChemComp-GOL:
GLYCEROL

Source
  • escherichia coli (E. coli)
KeywordsHYDROLASE / Beta-lactamase CTX-M-14 / hydrolase/antibiotic / hydrolase-antibiotic complex / hydrolase-hydrolase inhibitor complex

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