6Z1F
CryoEM structure of Rubisco Activase with its substrate Rubisco from Nostoc sp. (strain PCC7120)
Summary for 6Z1F
| Entry DOI | 10.2210/pdb6z1f/pdb |
| EMDB information | 11028 |
| Descriptor | Ribulose bisphosphate carboxylase/oxygenase activase, Ribulose bisphosphate carboxylase large chain, Ribulose bisphosphate carboxylase small chain, ... (7 entities in total) |
| Functional Keywords | aaa+, beta barrel, chaperone |
| Biological source | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) More |
| Total number of polymer chains | 22 |
| Total formula weight | 730434.60 |
| Authors | Wang, H.,Bracher, A.,Flecken, M.,Popilka, L.,Hartl, F.U.,Hayer-Hartl, M. (deposition date: 2020-05-13, release date: 2020-09-23, Last modification date: 2025-04-09) |
| Primary citation | Flecken, M.,Wang, H.,Popilka, L.,Hartl, F.U.,Bracher, A.,Hayer-Hartl, M. Dual Functions of a Rubisco Activase in Metabolic Repair and Recruitment to Carboxysomes. Cell, 183:457-473.e20, 2020 Cited by PubMed Abstract: 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. PubMed: 32979320DOI: 10.1016/j.cell.2020.09.010 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.86 Å) |
Structure validation
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