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Structure paper

TitleEpistasis arises from shifting the rate-limiting step during enzyme evolution of a beta-lactamase.
Journal, issue, pagesNat Catal, Vol. 7, Page 499-509, Year 2024
Publish dateJun 13, 2023 (structure data deposition date)
AuthorsFrohlich, C. / Bunzel, H.A. / Buda, K. / Mulholland, A.J. / van der Kamp, M.W. / Johnsen, P.J. / Leiros, H.S. / Tokuriki, N.
External linksNat Catal / PubMed:38828429
MethodsX-ray diffraction
Resolution1.17 - 2.66 Å
Structure data

PDB-8pea:
OXA-48_F72L. Epistasis Arises from Shifting the Rate-Limiting Step during Enzyme Evolution
Method: X-RAY DIFFRACTION / Resolution: 1.97 Å

PDB-8peb:
OXA-48_Q5. Epistasis Arises from Shifting the Rate-Limiting Step during Enzyme Evolution
Method: X-RAY DIFFRACTION / Resolution: 1.17 Å

PDB-8pec:
OXA-48_Q5-CAZ. Epistasis Arises from Shifting the Rate-Limiting Step during Enzyme Evolution
Method: X-RAY DIFFRACTION / Resolution: 2.66 Å

Chemicals

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-MLI:
MALONATE ION

ChemComp-CTJ:
1-({(2R)-2-[(1R)-1-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}-2-oxoethyl]-4-carboxy-3,6-dihydro-2H-1,3-thiazin-5-yl}methyl)pyridinium

Source
  • klebsiella pneumoniae (bacteria)
KeywordsHYDROLASE / Protein evolution. Antibiotic resistance. OXA-48. / Protein evolution. Antibiotic resistance. OXA-48. HYDROLASE. Serine-Beta-lactamase.

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