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-Structure paper
タイトル | Structure of green-type Rubisco activase from tobacco. |
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ジャーナル・号・ページ | Nat Struct Mol Biol, Vol. 18, Issue 12, Page 1366-1370, Year 2011 |
掲載日 | 2011年11月6日 |
著者 | Mathias Stotz / Oliver Mueller-Cajar / Susanne Ciniawsky / Petra Wendler / F Ulrich Hartl / Andreas Bracher / Manajit Hayer-Hartl / |
PubMed 要旨 | 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. |
リンク | Nat Struct Mol Biol / PubMed:22056769 |
手法 | EM (単粒子) / X線回折 |
解像度 | 2.95 - 20.0 Å |
構造データ | EMDB-1940: Negative stain EM density of green-type rubisco activase (R294V) from tobacco PDB-3t15: |
由来 |
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キーワード | PHOTOSYNTHESIS / Rubisco activase / AAA+ protein / NEGATIVE STAIN EM |