6smh | pdb_00006smh

Cryo-electron microscopy structure of a RbcL-Raf1 supercomplex from Synechococcus elongatus PCC 7942

spinqualitylabelsall models 6smh, resolution 4.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6smh is a 16 chain structure with sequence from Anacystis nidulans r2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: cbbL, rbcL, Synpcc7942_1426 (Anacystis nidulans R2), Synpcc7942_0833 (Anacystis nidulans R2) Activity: Ribulose-bisphosphate carboxylase, with EC number 4.1.1.39 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [RBL_SYNE7] RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. Publication Abstract from PubMed 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, Synechococcus elongatus 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, CO2-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 CO2-fixing modules to improve photosynthesis. Rubisco accumulation factor 1 (Raf1) plays essential roles in mediating Rubisco assembly and carboxysome biogenesis.,Huang F, Kong WW, Sun Y, Chen T, Dykes GF, Jiang YL, Liu LN Proc Natl Acad Sci U S A. 2020 Jul 7. pii: 2007990117. doi:, 10.1073/pnas.2007990117. PMID:32636267 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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