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Structure of Rubisco from Arabidopsis thaliana in complex with 2-carboxyarabinitol-1,5-bis­phosphate
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Molecular biophysics. (Molekylär biofysik)ORCID iD: 0000-0002-8642-9259
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Molecular biophysics. (Molecular Biophysics)ORCID iD: 0000-0001-8710-327x
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Molecular biophysics. (Molecular Biophysics)ORCID iD: 0000-0002-2729-0787
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Molecular biophysics. (Molecular Biophysics)ORCID iD: 0000-0003-2072-0884
2018 (English)In: ACTA CRYSTALLOGRAPHICA SECTION D: STRUCTURAL BIOLOGY, ISSN 2059-7983, Vol. 74, no 1, p. 1-9Article in journal (Refereed) Published
Abstract [en]

The crystal structure of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) from Arabidopsis thaliana is reported at 1.5 Å resolution. In light of the importance of A. thaliana as a model organism for understanding higher plant biology, and the pivotal role of Rubisco in photosynthetic carbon assimilation, there has been a notable absence of an A. thaliana Rubisco crystal structure. A. thaliana Rubisco is an L8S8 hexadecamer comprising eight plastome-encoded catalytic large (L) subunits and eight nuclear-encoded small (S) subunits. A. thaliana produces four distinct small-subunit isoforms (RbcS1A, RbcS1B, RbcS2B and RbcS3B), and this crystal structure provides a snapshot of A. thaliana Rubisco containing the low-abundance RbcS3B small-subunit isoform. Crystals were obtained in the presence of the transition-state analogue 2-carboxy-D-arabinitol-1,5-bisphosphate. A. thaliana Rubisco shares the overall fold characteristic of higher plant Rubiscos, but exhibits an interesting disparity between sequence and structural relatedness to other Rubisco isoforms. These results provide the structural framework to understand A. thaliana Rubisco and the potential catalytic differences that could be conferred by alternative A. thaliana Rubisco small-subunit isoforms.

Place, publisher, year, edition, pages
2018. Vol. 74, no 1, p. 1-9
Keywords [en]
ribulose-1, 5-bisphosphate, carboxylase/oxygenase, Rubisco, 2-carboxy­arabinitol-1, 5-bisphosphate, carbon fixation, Arabidopsis thaliana, rbcS multigene family, isoforms, merohedral twinning
National Category
Structural Biology
Research subject
Biology; Biology with specialization in Structural Biology
Identifiers
URN: urn:nbn:se:uu:diva-341464DOI: 10.1107/S2059798317017132ISI: 000423422400001PubMedID: 29372894OAI: oai:DiVA.org:uu-341464DiVA, id: diva2:1181583
Funder
Swedish Research Council, 2015-05007Available from: 2018-02-09 Created: 2018-02-09 Last updated: 2018-03-09Bibliographically approved

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