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Title1,2-Diol Dehydration by the Radical SAM Enzyme AprD4: A Matter of Proton Circulation and Substrate Flexibility.
Journal, issue, pagesJ. Am. Chem. Soc., Vol. 140, Page 1365-1371, Year 2018
Publish dateDec 21, 2017 (structure data deposition date)
AuthorsLiu, W.Q. / Amara, P. / Mouesca, J.M. / Ji, X. / Renoux, O. / Martin, L. / Zhang, C. / Zhang, Q. / Nicolet, Y.
External linksJ. Am. Chem. Soc. / PubMed:29300094
MethodsX-ray diffraction
Resolution2.55 Å
Structure data

PDB-6fd2:
Radical SAM 1,2-diol dehydratase AprD4 in complex with its substrate paromamine
Method: X-RAY DIFFRACTION / Resolution: 2.55 Å

Chemicals

ChemComp-D5E:
paromamine

ChemComp-SF4:
IRON/SULFUR CLUSTER

ChemComp-MET:
METHIONINE

ChemComp-5AD:
5'-DEOXYADENOSINE

ChemComp-HOH:
WATER

Source
  • streptoalloteichus tenebrarius (strain atcc 17920 / dsm 40477 / ncib 11028) (bacteria)
KeywordsBIOSYNTHETIC PROTEIN / Radical SAM / FeS-cluster containing enzyme / 1 / 2-diol dehydratase

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