PDBsum entry 1aa1

Oxidoreductase

PDB id: 1aa1

Contents

Protein chains

438 a.a. *

123 a.a. *

Ligands

3PG ×8

Metals

_MG ×4

Waters ×1008

* Residue conservation analysis

References listed in PDB file

Key reference

Title

Structure of a product complex of spinach ribulose-1,5-Bisphosphate carboxylase/oxygenase.

Authors

T.C.Taylor, I.Andersson.

Ref.

Biochemistry, 1997, 36, 4041-4046. [DOI no: 10.1021/bi962818w]

PubMed id

9092835

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.

Secondary reference #1

Title

Large structures at high resolution: the 1.6 a crystal structure of spinach ribulose-1,5-Bisphosphate carboxylase/oxygenase complexed with 2-Carboxyarabinitol bisphosphate.

Author

I.Andersson.

Ref.

J Mol Biol, 1996, 259, 160-174. [DOI no: 10.1006/jmbi.1996.0310]

PubMed id

8648644

Figure 1.
Figure 1. Reactions catalysed by rubisco.

Figure 7.
Figure 7. Overview of the active site of spinach rubisco showing 2-CABP, Mg 2+ and residues within hydrogen-bonding distance to these ligands. The hydroxyl groups at C2 and C3 of 2-CABP are in cis conformation. The two views in (a) and (b) are related by 180° with respect to the vertical axis.

The above figures are reproduced from the cited reference with permission from Elsevier