1RCO

SPINACH RUBISCO IN COMPLEX WITH THE INHIBITOR D-XYLULOSE-2,2-DIOL-1,5-BISPHOSPHATE

Summary for 1RCO

• Entry DOI: 10.2210/pdb1rco/pdb
• Descriptor: RIBULOSE BISPHOSPHATE CARBOXYLASE/OXYGENASE, D-XYLULOSE-2,2-DIOL-1,5-BISPHOSPHATE, ... (4 entities in total)
• Functional Keywords: lyase, carbon-carbon
• Biological source: Spinacia oleracea (spinach); More
• Cellular location: Plastid, chloroplast: P00875 P00870
• Total number of polymer chains: 16
• Total formula weight: 541611.65

Authors

Taylor, T.C.,Andersson, I. (deposition date: 1996-10-31, release date: 1997-03-12, Last modification date: 2024-10-30)

Primary citation

Taylor, T.C.,Fothergill, M.D.,Andersson, I.
A common structural basis for the inhibition of ribulose 1,5-bisphosphate carboxylase by 4-carboxyarabinitol 1,5-bisphosphate and xylulose 1,5-bisphosphate.
J.Biol.Chem., 271:32894-32899, 1996

PubMed Abstract: Ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) catalyzes the carboxylation of ribulose 1,5-bisphosphate. The reaction catalyzed by Rubisco involves several steps, some of which can occur as partial reactions, forming intermediates that can be isolated. Analogues of these intermediates are potent inhibitors of the enzyme. We have studied the interactions with the enzyme of two inhibitors, xylulose 1,5-bisphosphate and 4-carboxyarabinitol 1,5-bisphosphate, by x-ray crystallography. Crystals of the complexes were formed by cocrystallization under activating conditions. In addition, 4-carboxyarabinitol 1,5-bisphosphate was soaked into preformed activated crystals of the enzyme. The result of these experiments was the release of the activating CO2 molecule as well as the metal ion from the active site when the inhibitors bound to the enzyme. Comparison with the structure of an activated complex of the enzyme indicates that the structural basis for the release of the activator groups is a distortion of the metal binding site due to the different geometry of the C-3 hydroxyl of the inhibitors. Both inhibitors induce closure of active site loops despite the inactivated state of the enzyme. Xylulose 1,5-bisphosphate binds in a hydrated form at the active site.

PubMed: 8955130
DOI: 10.1074/jbc.271.51.32894

Experimental method

X-RAY DIFFRACTION (2.3 Å)