1AUS: Activated Unliganded Spinach Rubisco

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.
PDB ID: 1AUSDownload
MMDB ID: 48003
PDB Deposition Date: 1995/6/21
Updated in MMDB: 2012/10
Experimental Method:
x-ray diffraction
Resolution: 2.2  Å
Source Organism:
Similar Structures:
Biological Unit for 1AUS: hexadecameric; determined by author and by software (PISA)
Molecular Components in 1AUS
Label Count Molecule
Proteins (16 molecules)
Ribulose Bisphosphate Carboxylase/oxygenase(Gene symbol: rbcL)
Molecule annotation
Ribulose Bisphosphate Carboxylase/oxygenase
Molecule annotation
Chemicals (16 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB