Structure of Pisum sativum Rubisco with bound ribulose 1,5-bisphosphate

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Jan 1;69(Pt 1):10-4. doi: 10.1107/S1744309112047549. Epub 2012 Dec 25.


The first structure of a ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) from a pulse crop is reported. Rubisco was purified from Pisum sativum (garden pea) and diffraction-quality crystals were obtained by hanging-drop vapour diffusion in the presence of the substrate ribulose 1,5-bisphosphate. X-ray diffraction data were recorded to 2.20 Å resolution from a single crystal at the Canadian Light Source. The overall quaternary structure of non-activated P. sativum Rubisco highlights the conservation of the form I Rubisco hexadecameric complex. The electron density places the substrate in the active site at the interface of the large-subunit dimers. Lys201 in the active site is not carbamylated as expected for this non-activated structure. Some heterogeneity in the small-subunit sequence is noted, as well as possible variations in the conformation and contacts of ribulose 1,5-bisphosphate in the large-subunit active sites. Overall, the active-site conformation most closely correlates with the `closed' conformation observed in other substrate/inhibitor-bound Rubisco structures.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Catalytic Domain
  • Crystallography, X-Ray
  • Lysine / chemistry
  • Lysine / metabolism
  • Models, Molecular
  • Peas / enzymology*
  • Plant Proteins / chemistry
  • Plant Proteins / metabolism
  • Protein Conformation
  • Protein Multimerization
  • Ribulose-Bisphosphate Carboxylase / chemistry*
  • Ribulose-Bisphosphate Carboxylase / metabolism*
  • Ribulosephosphates / chemistry
  • Ribulosephosphates / metabolism*


  • Plant Proteins
  • Ribulosephosphates
  • ribulose-1,5 diphosphate
  • Ribulose-Bisphosphate Carboxylase
  • Lysine

Associated data

  • PDB/4HHH