Structural highlights
Publication Abstract from PubMed
Cells must cope with toxic or reactive intermediates formed during metabolism. One coping strategy is to sequester reactions that produce such intermediates within specialized compartments or tunnels connecting different active sites. Here, we show that propionyl-CoA synthase (PCS), an approximately 400-kDa homodimer, three-domain fusion protein and the key enzyme of the 3-hydroxypropionate bi-cycle for CO2 fixation, sequesters its reactive intermediate acrylyl-CoA. Structural analysis showed that PCS forms a multicatalytic reaction chamber. Kinetic analysis suggested that access to the reaction chamber and catalysis are synchronized by interdomain communication. The reaction chamber of PCS features three active sites and has a volume of only 33 nm(3). As one of the smallest multireaction chambers described in biology, PCS may inspire the engineering of a new class of dynamically regulated nanoreactors.
The multicatalytic compartment of propionyl-CoA synthase sequesters a toxic metabolite.,Bernhardsgrutter I, Vogeli B, Wagner T, Peter DM, Cortina NS, Kahnt J, Bange G, Engilberge S, Girard E, Riobe F, Maury O, Shima S, Zarzycki J, Erb TJ Nat Chem Biol. 2018 Oct 29. pii: 10.1038/s41589-018-0153-x. doi:, 10.1038/s41589-018-0153-x. PMID:30374166[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bernhardsgrutter I, Vogeli B, Wagner T, Peter DM, Cortina NS, Kahnt J, Bange G, Engilberge S, Girard E, Riobe F, Maury O, Shima S, Zarzycki J, Erb TJ. The multicatalytic compartment of propionyl-CoA synthase sequesters a toxic metabolite. Nat Chem Biol. 2018 Oct 29. pii: 10.1038/s41589-018-0153-x. doi:, 10.1038/s41589-018-0153-x. PMID:30374166 doi:https://dx.doi.org/10.1038/s41589-018-0153-x
