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-Structure paper
Title | Structure of green-type Rubisco activase from tobacco. |
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Journal, issue, pages | Nat Struct Mol Biol, Vol. 18, Issue 12, Page 1366-1370, Year 2011 |
Publish date | Nov 6, 2011 |
![]() | Mathias Stotz / Oliver Mueller-Cajar / Susanne Ciniawsky / Petra Wendler / F Ulrich Hartl / Andreas Bracher / Manajit Hayer-Hartl / ![]() |
PubMed Abstract | Rubisco, the enzyme that catalyzes the fixation of atmospheric CO(2) in photosynthesis, is subject to inactivation by inhibitory sugar phosphates. Here we report the 2.95-Å crystal structure of ...Rubisco, the enzyme that catalyzes the fixation of atmospheric CO(2) in photosynthesis, is subject to inactivation by inhibitory sugar phosphates. Here we report the 2.95-Å crystal structure of Nicotiana tabacum Rubisco activase (Rca), the enzyme that facilitates the removal of these inhibitors. Rca from tobacco has a classical AAA(+)-protein domain architecture. Although Rca populates a range of oligomeric states when in solution, it forms a helical arrangement with six subunits per turn when in the crystal. However, negative-stain electron microscopy of the active mutant R294V suggests that Rca functions as a hexamer. The residues determining species specificity for Rubisco are located in a helical insertion of the C-terminal domain and probably function in conjunction with the N-domain in Rubisco recognition. Loop segments exposed toward the central pore of the hexamer are required for the ATP-dependent remodeling of Rubisco, resulting in the release of inhibitory sugar. |
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Methods | EM (single particle) / X-ray diffraction |
Resolution | 2.95 - 20.0 Å |
Structure data | EMDB-1940: Negative stain EM density of green-type rubisco activase (R294V) from tobacco ![]() PDB-3t15: |
Source |
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![]() | PHOTOSYNTHESIS / Rubisco activase / AAA+ protein / NEGATIVE STAIN EM |