1AA1

ACTIVATED SPINACH RUBISCO IN COMPLEX WITH THE PRODUCT 3-PHOSPHOGLYCERATE

Summary for 1AA1

• Entry DOI: 10.2210/pdb1aa1/pdb
• Descriptor: RIBULOSE BISPHOSPHATE CARBOXYLASE (LARGE CHAIN), RIBULOSE BISPHOSPHATE CARBOXYLASE (SMALL CHAIN), MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: oxidoreductase, lyase (carbon-carbon)
• Biological source: Spinacia oleracea (spinach); More
• Cellular location: Plastid, chloroplast: P00875 Q43832
• Total number of polymer chains: 8
• Total formula weight: 271251.08

Authors

Taylor, T.C.,Andersson, I. (deposition date: 1997-01-20, release date: 1997-07-07, Last modification date: 2024-06-05)

Primary citation

Taylor, T.C.,Andersson, I.
Structure of a product complex of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase.
Biochemistry, 36:4041-4046, 1997

PubMed Abstract: The crystal structure of an activated complex of ribulose-1,5-bisphosphate carboxylase/oxygenase from spinach and its product 3-phosphoglycerate has been determined to 2.2 A resolution. The structure is of the open form with the active site accessible to the solvent as observed in the structures of the activated ligand-free enzyme and the complex of the activated enzyme with the substrate ribulose-1,5-bisphosphate. Two molecules of 3-phosphoglycerate are bound per active site. The phosphates of both molecules bind approximately at the same position as the phosphates of ribulose-1,5-bisphosphate or the six-carbon intermediate analogue 2-carboxyarabinitol-1,5-bisphosphate, but one product molecule is swung out from the active site with its carboxylate group pointing toward solution. The present structure points to direct participation of the active site side chain of lysine 175 in later stages of catalysis. This possibility is discussed in the light of mutagenesis studies.

PubMed: 9092835
DOI: 10.1021/bi962818w

Experimental method

X-RAY DIFFRACTION (2.2 Å)