4HHH

Structure of Pisum sativum Rubisco

Summary for 4HHH

• Entry DOI: 10.2210/pdb4hhh/pdb
• Descriptor: Ribulose bisphosphate carboxylase large chain, Ribulose bisphosphate carboxylase small chain, RIBULOSE-1,5-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: rubisco, ribulose-1, 5-bisphosphate, lyase
• Biological source: Pisum sativum (garden pea,peas); More
• Cellular location: Plastid, chloroplast: P04717
• Total number of polymer chains: 8
• Total formula weight: 271368.72

Authors

Loewen, P.C.,Didychuk, A.L.,Switala, J.,Loewen, M.C. (deposition date: 2012-10-09, release date: 2012-10-31, Last modification date: 2024-11-06)

Primary citation

Loewen, P.C.,Didychuk, A.L.,Switala, J.,Perez-Luque, R.,Fita, I.,Loewen, M.C.
Structure of Pisum sativum Rubisco with bound ribulose 1,5-bisphosphate.
Acta Crystallogr.,Sect.F, 69:10-14, 2013

PubMed Abstract: 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.

PubMed: 23295478
DOI: 10.1107/S1744309112047549

Experimental method

X-RAY DIFFRACTION (2.2 Å)