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Structure paper

TitleThe Structure of the Bifunctional Everninomicin Biosynthetic Enzyme EvdMO1 Suggests Independent Activity of the Fused Methyltransferase-Oxidase Domains.
Journal, issue, pagesBiochemistry, Vol. 57, Page 6827-6837, Year 2018
Publish dateAug 25, 2016 (structure data deposition date)
AuthorsStarbird, C.A. / Perry, N.A. / Chen, Q. / Berndt, S. / Yamakawa, I. / Loukachevitch, L.V. / Limbrick, E.M. / Bachmann, B.O. / Iverson, T.M. / McCulloch, K.M.
External linksBiochemistry / PubMed:30525509
MethodsX-ray diffraction
Resolution1.1004 - 3.35 Å
Structure data

PDB-5t38:
Crystal Structure of the N-terminal domain of EvdMO1 with SAH bound
Method: X-RAY DIFFRACTION / Resolution: 1.1502 Å

PDB-5t39:
Crystal Structure of the N-terminal domain of EvdMO1 in the presence of SAH and D-fucose
Method: X-RAY DIFFRACTION / Resolution: 1.1004 Å

PDB-6ec3:
Crystal Structure of EvdMO1
Method: X-RAY DIFFRACTION / Resolution: 3.35 Å

Chemicals

ChemComp-SAH:
S-ADENOSYL-L-HOMOCYSTEINE

ChemComp-HOH:
WATER

ChemComp-NI:
NICKEL (II) ION

ChemComp-BTB:
2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

Source
  • micromonospora carbonacea (bacteria)
KeywordsTRANSFERASE / methyltransferase / Rossmann-like fold / SAM-dependent / oxidoreductase / nonheme iron AKG-dependent oxygenase

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