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. 2018 Mar 29;46(12):6318–6329. doi: 10.1093/nar/gky233

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© The Author(s) 2018. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 8. — Model for autoinhibition, Edc3 alleviation and Edc3/Edc1 combined activation. (A) Autoinhibited conformation of the decapping holoenzyme. Dcp1 is yellow-gold, and the NRD and CD of Dcp2 are magenta and green, respectively. IM1&IM2, shown in red, stabilize this inactive conformation by making contacts with the core domains. The grey boxes are HLMs. (B) Edc3, shown in cyan, alleviated inhibition by binding to the HLMs, which disrupts the IM1&IM2 interaction with the Dcp1:Dcp2_core. (C) Representation of the activated Dcp1:Dcp2 structure where Edc1, orange, stabilizes a composite active site formed by the NRD and CD. Edc3 frees up the Dcp1:Edc1 binding site from IM1 & IM2.