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Structure paper

TitleThe multicatalytic compartment of propionyl-CoA synthase sequesters a toxic metabolite.
Journal, issue, pagesNat. Chem. Biol., Vol. 14, Page 1127-1132, Year 2018
Publish dateOct 13, 2017 (structure data deposition date)
AuthorsBernhardsgrutter, I. / Vogeli, B. / Wagner, T. / Peter, D.M. / Cortina, N.S. / Kahnt, J. / Bange, G. / Engilberge, S. / Girard, E. / Riobe, F. ...Bernhardsgrutter, I. / Vogeli, B. / Wagner, T. / Peter, D.M. / Cortina, N.S. / Kahnt, J. / Bange, G. / Engilberge, S. / Girard, E. / Riobe, F. / Maury, O. / Shima, S. / Zarzycki, J. / Erb, T.J.
External linksNat. Chem. Biol. / PubMed:30374166
MethodsX-ray diffraction
Resolution2.7 Å
Structure data

PDB-6eqo:
Tri-functional propionyl-CoA synthase of Erythrobacter sp. NAP1 with bound NADP+ and phosphomethylphosphonic acid adenylate ester
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

Chemicals

ChemComp-ACP:
PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / AMP-PCP, energy-carrying molecule analogue*YM

ChemComp-NAP:
NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

ChemComp-HOH:
WATER

Source
  • erythrobacter sp. nap1 (bacteria)
KeywordsOXIDOREDUCTASE / 3-hydroxpropionyl-CoA synthetase / 3-hydroxpropionyl-CoA dehydratase / acrylyl-CoA reductase / central carbon metabolism / carbon dioxode fixation / 3-hydroxypropionate bi-cycle / natural fusion enzyme / substrate channeling

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