3ZW6
MODEL OF HEXAMERIC AAA DOMAIN ARRANGEMENT OF GREEN-TYPE RUBISCO ACTIVASE FROM TOBACCO.
Summary for 3ZW6
| Entry DOI | 10.2210/pdb3zw6/pdb |
| Related | 3T15 |
| EMDB information | 1940 |
| Descriptor | RIBULOSE BISPHOSPHATE CARBOXYLASE/OXYGENASE ACTIVASE 1, CHLOROPLASTIC (1 entity in total) |
| Functional Keywords | photosynthesis, negative stain em |
| Biological source | NICOTIANA TABACUM (COMMON TOBACCO) |
| Total number of polymer chains | 6 |
| Total formula weight | 197140.81 |
| Authors | Stotz, M.,Mueller-Cajar, O.,Ciniawsky, S.,Wendler, P.,Hartl, F.U.,Bracher, A.,Hayer-Hartl, M. (deposition date: 2011-07-28, release date: 2011-11-09, Last modification date: 2024-05-08) |
| Primary citation | Stotz, M.,Mueller-Cajar, O.,Ciniawsky, S.,Wendler, P.,Hartl, F.U.,Bracher, A.,Hayer-Hartl, M. Structure of Green-Type Rubisco Activase from Tobacco Nat.Struct.Mol.Biol., 18:1366-, 2011 Cited by 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 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. PubMed: 22056769DOI: 10.1038/NSMB.2171 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (20 Å) |
Structure validation
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