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Structure paper

TitleBinding of Distinct Substrate Conformations Enables Hydroxylation of Remote Sites in Thaxtomin D by Cytochrome P450 TxtC.
Journal, issue, pagesJ. Am. Chem. Soc., Vol. 141, Page 216-222, Year 2019
Publish dateNov 17, 2017 (structure data deposition date)
AuthorsAlkhalaf, L.M. / Barry, S.M. / Rea, D. / Gallo, A. / Griffiths, D. / Lewandowski, J.R. / Fulop, V. / Challis, G.L.
External linksJ. Am. Chem. Soc. / PubMed:30516965
MethodsX-ray diffraction
Resolution1.7 - 2.8 Å
Structure data

PDB-6f0b:
Cytochrome P450 TxtC employs substrate conformational switching for sequential aliphatic and aromatic thaxtomin hydroxylation
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-6f0c:
Cytochrome P450 TxtC employs substrate conformational switching for sequential aliphatic and aromatic thaxtomin hydroxylation
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-C8H:
(3~{S},6~{S})-1,4-dimethyl-3-[(4-nitro-1~{H}-indol-3-yl)methyl]-6-(phenylmethyl)piperazine-2,5-dione

ChemComp-HOH:
WATER

ChemComp-C8B:
(3~{R},6~{S})-1,4-dimethyl-6-[(4-nitro-1~{H}-indol-3-yl)methyl]-3-oxidanyl-3-(phenylmethyl)piperazine-2,5-dione

ChemComp-OXY:
OXYGEN MOLECULE

Source
  • streptomyces acidiscabies 84-104 (bacteria)
KeywordsOXIDOREDUCTASE / Cytochrome P450 / TxtC / Thaxtomin hydroxylation

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