+検索条件
-Structure paper
タイトル | Identification and characterization of multiple rubisco activases in chemoautotrophic bacteria. |
---|---|
ジャーナル・号・ページ | Nat Commun, Vol. 6, Page 8883, Year 2015 |
掲載日 | 2015年11月16日 |
著者 | Yi-Chin Candace Tsai / Maria Claribel Lapina / Shashi Bhushan / Oliver Mueller-Cajar / |
PubMed 要旨 | Ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) is responsible for almost all biological CO2 assimilation, but forms inhibited complexes with its substrate ribulose-1,5-bisphosphate (RuBP) ...Ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) is responsible for almost all biological CO2 assimilation, but forms inhibited complexes with its substrate ribulose-1,5-bisphosphate (RuBP) and other sugar phosphates. The distantly related AAA+ proteins rubisco activase and CbbX remodel inhibited rubisco complexes to effect inhibitor release in plants and α-proteobacteria, respectively. Here we characterize a third class of rubisco activase in the chemolithoautotroph Acidithiobacillus ferrooxidans. Two sets of isoforms of CbbQ and CbbO form hetero-oligomers that function as specific activases for two structurally diverse rubisco forms. Mutational analysis supports a model wherein the AAA+ protein CbbQ functions as motor and CbbO is a substrate adaptor that binds rubisco via a von Willebrand factor A domain. Understanding the mechanisms employed by nature to overcome rubisco's shortcomings will increase our toolbox for engineering photosynthetic carbon dioxide fixation. |
リンク | Nat Commun / PubMed:26567524 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 23.0 Å |
構造データ | EMDB-6477: |
由来 |
|