6SMH
Cryo-electron microscopy structure of a RbcL-Raf1 supercomplex from Synechococcus elongatus PCC 7942
Summary for 6SMH
Entry DOI | 10.2210/pdb6smh/pdb |
EMDB information | 10235 |
Descriptor | Ribulose bisphosphate carboxylase large chain, Rubisco accumulation factor 1 (RAF1) peptide (2 entities in total) |
Functional Keywords | rubisco, rubisco accumulation factor1, raf1, synechococcus elongatus 7942, cyanobacteria, photosynthesis |
Biological source | Synechococcus elongatus (strain PCC 7942 / FACHB-805) More |
Total number of polymer chains | 16 |
Total formula weight | 570542.24 |
Authors | Huang, F.,Kong, W.-W.,Sun, Y.,Chen, T.,Dykes, G.F.,Jiang, Y.L.,Liu, L.N. (deposition date: 2019-08-21, release date: 2020-07-08, Last modification date: 2024-05-15) |
Primary citation | Huang, F.,Kong, W.W.,Sun, Y.,Chen, T.,Dykes, G.F.,Jiang, Y.L.,Liu, L.N. Rubisco accumulation factor 1 (Raf1) plays essential roles in mediating Rubisco assembly and carboxysome biogenesis. Proc.Natl.Acad.Sci.USA, 117:17418-17428, 2020 Cited by PubMed Abstract: Carboxysomes are membrane-free organelles for carbon assimilation in cyanobacteria. The carboxysome consists of a proteinaceous shell that structurally resembles virus capsids and internal enzymes including ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco), the primary carbon-fixing enzyme in photosynthesis. The formation of carboxysomes requires hierarchical self-assembly of thousands of protein subunits, initiated from Rubisco assembly and packaging to shell encapsulation. Here we study the role of Rubisco assembly factor 1 (Raf1) in Rubisco assembly and carboxysome formation in a model cyanobacterium, PCC7942 (Syn7942). Cryo-electron microscopy reveals that Raf1 facilitates Rubisco assembly by mediating RbcL dimer formation and dimer-dimer interactions. Syn7942 cells lacking Raf1 are unable to form canonical intact carboxysomes but generate a large number of intermediate assemblies comprising Rubisco, CcaA, CcmM, and CcmN without shell encapsulation and a low abundance of carboxysome-like structures with reduced dimensions and irregular shell shapes and internal organization. As a consequence, the Raf1-depleted cells exhibit reduced Rubisco content, CO-fixing activity, and cell growth. Our results provide mechanistic insight into the chaperone-assisted Rubisco assembly and biogenesis of carboxysomes. Advanced understanding of the biogenesis and stepwise formation process of the biogeochemically important organelle may inform strategies for heterologous engineering of functional CO-fixing modules to improve photosynthesis. PubMed: 32636267DOI: 10.1073/pnas.2007990117 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (4.3 Å) |
Structure validation
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