3T15

Structure of green-type Rubisco activase from tobacco

Summary for 3T15

• Entry DOI: 10.2210/pdb3t15/pdb
• Related: 3zw6
• EMDB information: 1940
• Descriptor: Ribulose bisphosphate carboxylase/oxygenase activase 1, chloroplastic (1 entity in total)
• Functional Keywords: photosynthesis, rubisco activase, aaa+ protein
• Biological source: Nicotiana tabacum (American tobacco,tobacco)
• Total number of polymer chains: 1
• Total formula weight: 32856.80

Authors

Stotz, M.,Wendler, P.,Mueller-Cajar, O.,Hartl, F.U.,Bracher, A.,Hayer-Hartl, M. (deposition date: 2011-07-21, release date: 2011-11-09, Last modification date: 2024-02-28)

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., 18:1366-1370, 2011

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: 22056769
DOI: 10.1038/nsmb.2171

Experimental method

X-RAY DIFFRACTION (2.95 Å)