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-Structure paper
Title | Cryo-EM reveals distinct conformations of ATP synthase on exposure to ATP. |
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Journal, issue, pages | Elife, Vol. 8, Year 2019 |
Publish date | Mar 26, 2019 |
Authors | Meghna Sobti / Robert Ishmukhametov / James C Bouwer / Anita Ayer / Cacang Suarna / Nicola J Smith / Mary Christie / Roland Stocker / Thomas M Duncan / Alastair G Stewart / |
PubMed Abstract | ATP synthase produces the majority of cellular energy in most cells. We have previously reported cryo-EM maps of autoinhibited ATP synthase imaged without addition of nucleotide (Sobti et al. 2016), ...ATP synthase produces the majority of cellular energy in most cells. We have previously reported cryo-EM maps of autoinhibited ATP synthase imaged without addition of nucleotide (Sobti et al. 2016), indicating that the subunit ε engages the α, β and γ subunits to lock the enzyme and prevent functional rotation. Here we present multiple cryo-EM reconstructions of the enzyme frozen after the addition of MgATP to identify the changes that occur when this ε inhibition is removed. The maps generated show that, after exposure to MgATP, ATP synthase adopts a different conformation with a catalytic subunit changing conformation substantially and the ε C-terminal domain transitioning via an intermediate 'half-up' state to a condensed 'down' state. This work provides direct evidence for unique conformational states that occur in ATP synthase when ATP binding prevents the ε C-terminal domain from entering the inhibitory 'up' state. |
External links | Elife / PubMed:30912741 / PubMed Central |
Methods | EM (single particle) |
Resolution | 5.0 - 7.22 Å |
Structure data | EMDB-20006: EMDB-20007: EMDB-20008: EMDB-9345: EMDB-9346: EMDB-9348: |
Source |
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