Journal
NATURE CHEMICAL BIOLOGY
Volume 14, Issue 12, Pages 1127-+Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/s41589-018-0153-x
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Funding
- DOE Office of Science User Facility [DE-AC02-05CH11231]
- Deutsche Forschungsgemeinschaft through Collaborative Research Centre [SFB 987]
- European Research Council [ERC 637675]
- FET-Open Grant [686330]
- Gebert-Ruf-Stiftung [GRS 062-12]
- Max-Planck-Society
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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 similar to 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.
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