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Structure paper

TitleCatalytic mechanism and molecular engineering of quinolone biosynthesis in dioxygenase AsqJ.
Journal, issue, pagesNat Commun, Vol. 9, Page 1168-1168, Year 2018
Publish dateJun 20, 2017 (structure data deposition date)
AuthorsMader, S.L. / Brauer, A. / Groll, M. / Kaila, V.R.I.
External linksNat Commun / PubMed:29563492
MethodsX-ray diffraction
Resolution1.55 - 1.75 Å
Structure data

PDB-5oa4:
Fe(II)/(alpha)ketoglutarate-dependent dioxygenase AsqJ_V72I mutant in complex with 4-methoxycyclopeptin (1)
Method: X-RAY DIFFRACTION / Resolution: 1.55 Å

PDB-5oa7:
Fe(II)/(alpha)ketoglutarate-dependent dioxygenase AsqJ_V72I mutant in complex with cyclopeptin (1b)
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

PDB-5oa8:
Fe(II)/(alpha)ketoglutarate-dependent dioxygenase AsqJ_V72I mutant in complex with demethylated cyclopeptin (1d)
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

PDB-6eoz:
Fe(II)/(alpha)ketoglutarate-dependent dioxygenase AsqJ_V72K mutant in complex with cyclopeptin (1b)
Method: X-RAY DIFFRACTION / Resolution: 1.55 Å

Chemicals

ChemComp-NI:
NICKEL (II) ION

ChemComp-58D:
(3S)-3-(4-methoxybenzyl)-4-methyl-3,4-dihydro-1H-1,4-benzodiazepine-2,5-dione

ChemComp-TRS:
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-AKG:
2-OXOGLUTARIC ACID

ChemComp-58K:
cyclopeptin

ChemComp-58L:
demethylated cyclopeptin

Source
  • emericella nidulans (strain fgsc a4 / atcc 38163 / cbs 112.46 / nrrl 194 / m139) (mold)
KeywordsOXIDOREDUCTASE / Antibiotics / Quinolone Biosynthesis / Molecular Engineering / Desaturase / Catalytic Mechanism / Mutagenesis / pi-stacking

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