Journal:Acta Cryst F:S2053230X19002693
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(Difference between revisions)
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Regulation of PRK enzyme activity in response to light controls carbon fixation during photosynthesis. This occurs via reversible formation of disulfide bonds during dark inactivation and complex formation with the adaptor protein CP12 and glyceraldehyde-3-phosphate dehydrogenase, another CBB cycle enzyme. Interestingly, we find a disulphide bond between Cys40 and the P-loop residue Cys18 in our crystal structure, revealing the structural basis for redox-inactivation of PRK activity. A second disulphide bond appears to rigidify the dimer interface and may thereby contribute to regulation by the adaptor protein CP12 and glyceraldehyde-3-phosphate dehydrogenase into a supramolecular complex within which both enzymes are inhibited. | Regulation of PRK enzyme activity in response to light controls carbon fixation during photosynthesis. This occurs via reversible formation of disulfide bonds during dark inactivation and complex formation with the adaptor protein CP12 and glyceraldehyde-3-phosphate dehydrogenase, another CBB cycle enzyme. Interestingly, we find a disulphide bond between Cys40 and the P-loop residue Cys18 in our crystal structure, revealing the structural basis for redox-inactivation of PRK activity. A second disulphide bond appears to rigidify the dimer interface and may thereby contribute to regulation by the adaptor protein CP12 and glyceraldehyde-3-phosphate dehydrogenase into a supramolecular complex within which both enzymes are inhibited. | ||
| - | Perpendicular views of the asymmetric unit in the Syn6301-PRK crystal lattice | + | Perpendicular views of the asymmetric unit in the Syn6301-PRK crystal lattice: |
*<scene name='80/809165/Cv/2'>First view</scene>. | *<scene name='80/809165/Cv/2'>First view</scene>. | ||
*<scene name='80/809165/Cv/3'>Second view</scene>. | *<scene name='80/809165/Cv/3'>Second view</scene>. | ||
| + | The PRK chains A and B are shown as green and yellow ribbons, respectively. The disulphide bonds are represented as yellow sticks. N- and C-termini are indicated. | ||
<b>References</b><br> | <b>References</b><br> | ||
Revision as of 11:12, 26 February 2019
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