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-Structure paper
タイトル | Dual Functions of a Rubisco Activase in Metabolic Repair and Recruitment to Carboxysomes. |
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ジャーナル・号・ページ | Cell, Vol. 183, Issue 2, Page 457-473.e20, Year 2020 |
掲載日 | 2020年10月15日 |
著者 | Mirkko Flecken / Huping Wang / Leonhard Popilka / F Ulrich Hartl / Andreas Bracher / Manajit Hayer-Hartl / |
PubMed 要旨 | Rubisco, the key enzyme of CO fixation in photosynthesis, is prone to inactivation by inhibitory sugar phosphates. Inhibited Rubisco undergoes conformational repair by the hexameric AAA+ chaperone ...Rubisco, the key enzyme of CO fixation in photosynthesis, is prone to inactivation by inhibitory sugar phosphates. Inhibited Rubisco undergoes conformational repair by the hexameric AAA+ chaperone Rubisco activase (Rca) in a process that is not well understood. Here, we performed a structural and mechanistic analysis of cyanobacterial Rca, a close homolog of plant Rca. In the Rca:Rubisco complex, Rca is positioned over the Rubisco catalytic site under repair and pulls the N-terminal tail of the large Rubisco subunit (RbcL) into the hexamer pore. Simultaneous displacement of the C terminus of the adjacent RbcL opens the catalytic site for inhibitor release. An alternative interaction of Rca with Rubisco is mediated by C-terminal domains that resemble the small Rubisco subunit. These domains, together with the N-terminal AAA+ hexamer, ensure that Rca is packaged with Rubisco into carboxysomes. The cyanobacterial Rca is a dual-purpose protein with functions in Rubisco repair and carboxysome organization. |
リンク | Cell / PubMed:32979320 |
手法 | EM (単粒子) / X線回折 |
解像度 | 1.38 - 8.2 Å |
構造データ | EMDB-11028, PDB-6z1f: EMDB-11029, PDB-6z1g: EMDB-11575: PDB-6has: PDB-6z1d: PDB-6z1e: |
化合物 | ChemComp-NI: ChemComp-HOH: ChemComp-GD: ChemComp-CL: ChemComp-ADP: ChemComp-AGS: ChemComp-MG: ChemComp-CAP: |
由来 |
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キーワード | CHAPERONE / alpha-beta structure / Rubisco / AAA+ domain / AAA+ / beta barrel / PHOTOSYNTHESIS |