6EQO

Tri-functional propionyl-CoA synthase of Erythrobacter sp. NAP1 with bound NADP+ and phosphomethylphosphonic acid adenylate ester

Summary for 6EQO

Entry DOI	10.2210/pdb6eqo/pdb
Descriptor	Acetyl-coenzyme A synthetase, PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (4 entities in total)
Functional Keywords	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, oxidoreductase
Biological source	Erythrobacter sp. NAP1
Total number of polymer chains	2
Total formula weight	403752.44
Authors	Zarzycki, J.,Bernhardsgruetter, I.,Voegeli, B.,Wagner, T.,Engilberge, S.,Girard, E.,Shima, S.,Erb, T.J. (deposition date: 2017-10-13, release date: 2018-10-24, Last modification date: 2018-11-28)
Primary citation	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. The multicatalytic compartment of propionyl-CoA synthase sequesters a toxic metabolite. Nat. Chem. Biol., 14:1127-1132, 2018 Cited by PubMed: 30374166 DOI: 10.1038/s41589-018-0153-x PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.7 Å)

Structure validation