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TitleHinge-shift mechanism as a protein design principle for the evolution of beta-lactamases from substrate promiscuity to specificity.
Journal, issue, pagesNat Commun, Vol. 12, Page 1852-1852, Year 2021
Publish dateApr 20, 2020 (structure data deposition date)
AuthorsModi, T. / Risso, V.A. / Martinez-Rodriguez, S. / Gavira, J.A. / Mebrat, M.D. / Van Horn, W.D. / Sanchez-Ruiz, J.M. / Banu Ozkan, S.
External linksNat Commun / PubMed:33767175
MethodsX-ray diffraction
Resolution1.7 Å
Structure data

PDB-6yrs:
Structure of a new variant of GNCA ancestral beta-lactamase
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-ACT:
ACETATE ION

ChemComp-PGE:
TRIETHYLENE GLYCOL

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-SO4:
SULFATE ION

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-HOH:
WATER

Source
  • synthetic construct (others)
KeywordsHYDROLASE / ANTIBIOTIC RESISTANCE / ANCESTRAL RECONSTRUCTED

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