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TitleStructural insights into 2-oxindole-forming monooxygenase MarE: Divergent architecture and substrate positioning versus tryptophan dioxygenases.
Journal, issue, pagesJ. Biol. Chem., Vol. 301, Page 108241-108241, Year 2025
Publish dateFeb 9, 2024 (structure data deposition date)
AuthorsShin, I. / Nguyen, R.C. / Montoya, S.R. / Liu, A.
External linksJ. Biol. Chem. / PubMed:39880093
MethodsX-ray diffraction
Resolution1.89 - 2.45 Å
Structure data

PDB-8vyy:
The crystal structure of MarE in complex with its native substrate, beta-methyl-L-tryptophan
Method: X-RAY DIFFRACTION / Resolution: 2.45 Å

PDB-9ca3:
Crystal structure of MarE C280S in complex with cyanide bound heme and its native substrate, beta-methyl-L-tryptophan
Method: X-RAY DIFFRACTION / Resolution: 1.89 Å

Chemicals

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-78U:
(betaS)-beta-methyl-L-tryptophan

ChemComp-HOH:
WATER

ChemComp-CYN:
CYANIDE ION

Source
  • streptomyces sp. (bacteria)
  • streptomyces sp. b9173 (bacteria)
KeywordsOXIDOREDUCTASE / Oxygenase / Monooxygenase / Heme-dependent aromatic oxygenase (HDAO) / heme-dependent aromatic oxygenase / HDAO / heme / cyanide / beta-methyl-L-tryptophan

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