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8BDB

Ribulose-1,5-bisphosphate carboxylase/oxygenase from Griffithsia monilis

Summary for 8BDB
Entry DOI10.2210/pdb8bdb/pdb
DescriptorRibulose bisphosphate carboxylase large chain, Ribulose bisphosphate carboxylase small chain, MAGNESIUM ION, ... (8 entities in total)
Functional Keywordscarbon dioxide fixation, photorespiration, lyase (carbon-carbon), photosynthesis
Biological sourceGriffithsia monilis
More
Total number of polymer chains16
Total formula weight571318.61
Authors
Andersson, I.,Gunn, L.H. (deposition date: 2022-10-19, release date: 2023-06-14, Last modification date: 2024-02-07)
Primary citationZhou, Y.,Gunn, L.H.,Birch, R.,Andersson, I.,Whitney, S.M.
Grafting Rhodobacter sphaeroides with red algae Rubisco to accelerate catalysis and plant growth.
Nat.Plants, 9:978-986, 2023
Cited by
PubMed Abstract: Improving the carboxylation properties of Rubisco has primarily arisen from unforeseen amino acid substitutions remote from the catalytic site. The unpredictability has frustrated rational design efforts to enhance plant Rubisco towards the prized growth-enhancing carboxylation properties of red algae Griffithsia monilis GmRubisco. To address this, we determined the crystal structure of GmRubisco to 1.7 Å. Three structurally divergent domains were identified relative to the red-type bacterial Rhodobacter sphaeroides RsRubisco that, unlike GmRubisco, are expressed in Escherichia coli and plants. Kinetic comparison of 11 RsRubisco chimaeras revealed that incorporating C329A and A332V substitutions from GmRubisco Loop 6 (corresponding to plant residues 328 and 331) into RsRubisco increased the carboxylation rate (k) by 60%, the carboxylation efficiency in air by 22% and the CO/O specificity (S) by 7%. Plastome transformation of this RsRubisco Loop 6 mutant into tobacco enhanced photosynthesis and growth up to twofold over tobacco producing wild-type RsRubisco. Our findings demonstrate the utility of RsRubisco for the identification and in planta testing of amino acid grafts from algal Rubisco that can enhance the enzyme's carboxylase potential.
PubMed: 37291398
DOI: 10.1038/s41477-023-01436-7
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation

237992

数据于2025-06-25公开中

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