4wt5

The C-terminal domain of Rubisco Accumulation Factor 1 from Arabidopsis thaliana, crystal form II

spinqualitylabelsall models 4wt5, resolution 2.57Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4wt5 is a 2 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.568Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RAF2_ARATH Required for assembly or stability of RuBisCO. Acts at a postchaperonin step to fold and/or assemble the large subunit (LS) into RuBisCO (By similarity). Publication Abstract from PubMed Biogenesis of the photosynthetic enzyme Rubisco, a complex of eight large (RbcL) and eight small (RbcS) subunits, requires assembly chaperones. Here we analyzed the role of Rubisco accumulation factor1 (Raf1), a dimer of approximately 40-kDa subunits. We find that Raf1 from Synechococcus elongatus acts downstream of chaperonin-assisted RbcL folding by stabilizing RbcL antiparallel dimers for assembly into RbcL8 complexes with four Raf1 dimers bound. Raf1 displacement by RbcS results in holoenzyme formation. Crystal structures show that Raf1 from Arabidopsis thaliana consists of a beta-sheet dimerization domain and a flexibly linked alpha-helical domain. Chemical cross-linking and EM reconstruction indicate that the beta-domains bind along the equator of each RbcL2 unit, and the alpha-helical domains embrace the top and bottom edges of RbcL2. Raf1 fulfills a role similar to that of the assembly chaperone RbcX, thus suggesting that functionally redundant factors ensure efficient Rubisco biogenesis. Structure and mechanism of the Rubisco-assembly chaperone Raf1.,Hauser T, Bhat JY, Milicic G, Wendler P, Hartl FU, Bracher A, Hayer-Hartl M Nat Struct Mol Biol. 2015 Aug 3. doi: 10.1038/nsmb.3062. PMID:26237510 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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