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Structure paper

TitleA single diiron enzyme catalyses the oxidative rearrangement of tryptophan to indole nitrile.
Journal, issue, pagesNat. Chem., Vol. 16, Page 1989-1998, Year 2024
Publish dateAug 21, 2023 (structure data deposition date)
AuthorsAdak, S. / Ye, N. / Calderone, L.A. / Duan, M. / Lubeck, W. / Schafer, R.J.B. / Lukowski, A.L. / Houk, K.N. / Pandelia, M.E. / Drennan, C.L. / Moore, B.S.
External linksNat. Chem. / PubMed:39285206
MethodsX-ray diffraction
Resolution2 - 2.3 Å
Structure data

PDB-8twn:
Crystal structure of nitrile synthase AetD with substrate bound
Method: X-RAY DIFFRACTION / Resolution: 2.08 Å

PDB-8twt:
Crystal structure of nitrile synthase AetD with substrate bound and cofactor partially assembled
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-8tww:
Crystal structure of nitrile synthase AetD with substrate bound and cofactor fully assembled
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-67I:
(2S)-2-azanyl-3-[5,7-bis(bromanyl)-1H-indol-3-yl]propanoic acid

ChemComp-MLT:
D-MALATE

ChemComp-HOH:
WATER

ChemComp-SIN:
SUCCINIC ACID

ChemComp-FE:
Unknown entry

ChemComp-GOL:
GLYCEROL

Source
  • aetokthonos hydrillicola (bacteria)
KeywordsOXIDOREDUCTASE / nitrile synthase / non-heme iron enzyme / diiron enzyme

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