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@article{McFarlane:2018:10.1101/414334,
author = {McFarlane, C and Shah, N and Kabasakal, B and Cotton, CAR and Bubeck, D and Murray, J},
doi = {10.1101/414334},
journal = {biorxiv},
title = {Structural basis of light-induced redox regulation in the Calvin cycle},
url = {http://dx.doi.org/10.1101/414334},
year = {2018}
}

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TY  - JOUR
AB  - Abstract In plants, carbon dioxide is fixed via the Calvin cycle in a tightly regulated process. Key to this regulation is the conditionally disordered protein CP12. CP12 forms a complex with two Calvin cycle enzymes, glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and phosphoribulokinase (PRK), inhibiting their activities. The mode of CP12 action was unknown. By solving crystal structures of CP12 bound to GAPDH, and the ternary GAPDH-CP12-PRK complex by electron cryo-microscopy, we reveal that formation of the N-terminal disulfide pre-orders CP12 prior to binding the PRK active site. We find that CP12 binding to GAPDH influences substrate accessibility of all GAPDH active sites in the binary and ternary inhibited complexes. Our model explains how CP12 integrates responses from both redox state and nicotinamide dinucleotide availability to regulate carbon fixation. One Sentence Summary How plants turn off carbon fixation in the dark.
AU  - McFarlane,C
AU  - Shah,N
AU  - Kabasakal,B
AU  - Cotton,CAR
AU  - Bubeck,D
AU  - Murray,J
DO  - 10.1101/414334
PY  - 2018///
TI  - Structural basis of light-induced redox regulation in the Calvin cycle
T2  - biorxiv
UR  - http://dx.doi.org/10.1101/414334
ER  -

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