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Structure paper

TitleMultiple substitutions lead to increased loop flexibility and expanded specificity in Acinetobacter baumannii carbapenemase OXA-239.
Journal, issue, pagesBiochem. J., Vol. 475, Page 273-288, Year 2018
Publish dateJul 18, 2017 (structure data deposition date)
AuthorsHarper, T.M. / June, C.M. / Taracila, M.A. / Bonomo, R.A. / Powers, R.A. / Leonard, D.A.
External linksBiochem. J. / PubMed:29229762
MethodsX-ray diffraction
Resolution1.81 - 1.87 Å
Structure data

PDB-5wi3:
Structure of Acinetobacter baumannii carbapenemase OXA-239 K82D bound to cefotaxime
Method: X-RAY DIFFRACTION / Resolution: 1.81 Å

PDB-5wi7:
Structure of Acinetobacter baumannii carbapenemase OXA-239 K82D bound to doripenem
Method: X-RAY DIFFRACTION / Resolution: 1.861 Å

PDB-5wib:
Structure of Acinetobacter baumannii carbapenemase OXA-239 K82D bound to imipenem
Method: X-RAY DIFFRACTION / Resolution: 1.87 Å

Chemicals

ChemComp-CEF:
CEFOTAXIME, C3' cleaved, open, bound form / antibiotic*YM

ChemComp-HOH:
WATER

ChemComp-4J6:
(4R,5S)-5-[(2S,3R)-3-hydroxy-1-oxobutan-2-yl]-4-methyl-3-({(3S,5S)-5-[(sulfamoylamino)methyl]pyrrolidin-3-yl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid

ChemComp-ID1:
Imipenem / antibiotic*YM

Source
  • acinetobacter sp. enrichment culture clone 8407 (environmental samples)
KeywordsHYDROLASE / beta-lactamase / antibiotic resistance

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