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

Alternative titleStructure of non-activated Pisum sativum Rubisco in complex with its substrate ribulose-1,5-bisphosphate
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DOIResolve DOI: http://doi.org/10.1107/S1744309112047549
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TypeArticle
Journal titleActa Crystallographica Section F Structural Biology and Crystallization Communications
ISSN1744-3091
Volume69
Issue1
Pages1014; # of pages: 5
Subjectmolecular replacement; Pisum sativum; ribulose 1,5-bisphosphate; Rubisco
AbstractThe 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 date
PublisherInternational Union of Crystallography
LanguageEnglish
AffiliationAquatic and Crop Resource Development; National Research Council Canada
Peer reviewedYes
NRC number55421
NPARC number21268467
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Record identifierc8dc6913-970d-4981-9cfc-661968ce8fac
Record created2013-07-24
Record modified2016-05-09
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