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8Q05

Chlorella sorokiniana Rubisco with CsLinker (alpha3-alpha4) bound: D4 symmetry expanded

Summary for 8Q05
Entry DOI10.2210/pdb8q05/pdb
EMDB information18050
DescriptorCsLinker (alpha3-alpha4), Ribulose bisphosphate carboxylase large chain, Ribulose bisphosphate carboxylase small subunit, chloroplastic, ... (4 entities in total)
Functional Keywordsrubisco, plant protein
Biological sourceChlorella sorokiniana
More
Total number of polymer chains17
Total formula weight599158.26
Authors
Barrett, J.,Blaza, J.N.,Mackinder, L.C.M. (deposition date: 2023-07-27, release date: 2024-08-07, Last modification date: 2024-10-30)
Primary citationBarrett, J.,Naduthodi, M.I.S.,Mao, Y.,Degut, C.,Musial, S.,Salter, A.,Leake, M.C.,Plevin, M.J.,McCormick, A.J.,Blaza, J.N.,Mackinder, L.C.M.
A promiscuous mechanism to phase separate eukaryotic carbon fixation in the green lineage.
Nat.Plants, 2024
Cited by
PubMed Abstract: CO fixation is commonly limited by inefficiency of the CO-fixing enzyme Rubisco. Eukaryotic algae concentrate and fix CO in phase-separated condensates called pyrenoids, which complete up to one-third of global CO fixation. Condensation of Rubisco in pyrenoids is dependent on interaction with disordered linker proteins that show little conservation between species. We developed a sequence-independent bioinformatic pipeline to identify linker proteins in green algae. We report the linker from Chlorella and demonstrate that it binds a conserved site on the Rubisco large subunit. We show that the Chlorella linker phase separates Chlamydomonas Rubisco and that despite their separation by ~800 million years of evolution, the Chlorella linker can support the formation of a functional pyrenoid in Chlamydomonas. This cross-species reactivity extends to plants, with the Chlorella linker able to drive condensation of some native plant Rubiscos in vitro and in planta. Our results represent an exciting frontier for pyrenoid engineering in plants, which is modelled to increase crop yields.
PubMed: 39384944
DOI: 10.1038/s41477-024-01812-x
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.77 Å)
Structure validation

227344

數據於2024-11-13公開中

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