6KKN

Crystal structure of RuBisCO accumulation factor Raf1 from Anabaena sp. PCC 7120

Summary for 6KKN

• Entry DOI: 10.2210/pdb6kkn/pdb
• Descriptor: All5250 protein (1 entity in total)
• Functional Keywords: rubisco, chaperone, raf1
• Biological source: Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) (Anabaena sp. PCC 7120)
• Total number of polymer chains: 1
• Total formula weight: 42856.03

Authors

Xia, L.Y.,Jiang, Y.L.,Kong, W.W.,Chen, Y.,Zhou, C.Z. (deposition date: 2019-07-26, release date: 2020-05-13, Last modification date: 2023-11-22)

Primary citation

Xia, L.Y.,Jiang, Y.L.,Kong, W.W.,Sun, H.,Li, W.F.,Chen, Y.,Zhou, C.Z.
Molecular basis for the assembly of RuBisCO assisted by the chaperone Raf1.
Nat.Plants, 6:708-717, 2020

PubMed Abstract: The folding and assembly of RuBisCO, the most abundant enzyme in nature, needs a series of chaperones, including the RuBisCO accumulation factor Raf1, which is highly conserved in cyanobacteria and plants. Here, we report the crystal structures of Raf1 from cyanobacteria Anabaena sp. PCC 7120 and its complex with RuBisCO large subunit RbcL. Structural analyses and biochemical assays reveal that each Raf1 dimer captures an RbcL dimer, with the C-terminal tail inserting into the catalytic pocket, and further mediates the assembly of RbcL dimers to form the octameric core of RuBisCO. Furthermore, the cryo-electron microscopy structures of the RbcL-Raf1-RbcS assembly intermediates enable us to see a dynamic assembly process from RbcLRaf1 to the holoenzyme RbcLRbcS. In vitro assays also indicate that Raf1 can attenuate and reverse CcmM-mediated cyanobacterial RuBisCO condensation. Combined with previous findings, we propose a putative model for the assembly of cyanobacterial RuBisCO coordinated by the chaperone Raf1.

PubMed: 32451445
DOI: 10.1038/s41477-020-0665-8

Experimental method

X-RAY DIFFRACTION (2.85 Å)