Structure of green-type Rubisco activase from tobacco

• Published in: Nature structural & molecular biology Vol. 18; no. 12; pp. 1366 - 1370
• Main Authors: Stotz, Mathias, Mueller-Cajar, Oliver, Ciniawsky, Susanne, Wendler, Petra, Hartl, F Ulrich, Bracher, Andreas, Hayer-Hartl, Manajit
• Format: Journal Article
• Language: English
• Published: New York Nature Publishing Group US 01.12.2011; Nature Publishing Group
• Subjects: 631/337/470; 631/45/535; 631/45/607; Adenosine triphosphatase; Amino Acid Sequence; ATP; Biochemistry; Biological Microscopy; Biomedical and Life Sciences; Carbon dioxide fixation; Crystal structure; Crystallography, X-Ray; Electron microscopy; Enzymes; Genetic aspects; Inactivation; Life Sciences; Membrane Biology; Models, Molecular; Molecular Sequence Data; Molecular structure; Nicotiana - enzymology; Nicotiana - metabolism; Phosphates; Photosynthesis; Photosynthesis - physiology; Physiological aspects; Plant Proteins - chemistry; Plant Proteins - physiology; Protein Structure; Protein Structure, Tertiary; Ribulose-Bisphosphate Carboxylase - metabolism; Rubisco; Sequence Alignment; Sugar; Tissue Plasminogen Activator - chemistry; Tissue Plasminogen Activator - physiology; Tobacco; Tobacco (Plant); Germany

The enzyme Rubisco has a central role in atmospheric CO 2 fixation. Rubisco can be inactivated if its sugar substrate is bound prior to carbamylation of a residue in the active site. The structure of tobacco Rca, the enzyme that removes the bound sugar substrate and activates Rubisco, is now present...