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Structure paper

TitleStudies on enmetazobactam clarify mechanisms of widely used beta-lactamase inhibitors.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 119, Page e2117310119-e2117310119, Year 2022
Publish dateOct 10, 2019 (structure data deposition date)
AuthorsLang, P.A. / Raj, R. / Tumber, A. / Lohans, C.T. / Rabe, P. / Robinson, C.V. / Brem, J. / Schofield, C.J.
External linksProc. Natl. Acad. Sci. USA / PubMed:35486701
MethodsX-ray diffraction
Resolution1.598 - 1.85 Å
Structure data

PDB-6t35:
Crystal structure of AmpC from E.coli with Enmetazobactam (AAI-101)
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

PDB-7b3r:
OXA-10 beta-lactamase with S64Dha modification and lysinoalanine crosslink
Method: X-RAY DIFFRACTION / Resolution: 1.83 Å

PDB-7b3s:
OXA-10 beta-lactamase with S67Dha modification
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-7b3u:
OXA-10 beta-lactamase with covalent modification
Method: X-RAY DIFFRACTION / Resolution: 1.598 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-M9W:
Enmetazobactam derived trans-enamine adduct.

ChemComp-ZN:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-NA:
Unknown entry

ChemComp-CO2:
CARBON DIOXIDE

Source
  • escherichia coli k-12 (bacteria)
  • pseudomonas aeruginosa (bacteria)
KeywordsHYDROLASE / beta lactamase / antibiotic resistance / antimicrobial protein / mechanism based inhibitor / tazobactam / dehydroalanine / irreversible inhibition / covalent modification

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