4WT3

The N-terminal domain of Rubisco Accumulation Factor 1 from Arabidopsis thaliana

Summary for 4WT3

• Entry DOI: 10.2210/pdb4wt3/pdb
• Descriptor: Rubisco Accumulation Factor 1, isoform 2 (2 entities in total)
• Functional Keywords: assembly chaperone, chaperone
• Biological source: Arabidopsis thaliana (Mouse-ear cress)
• Cellular location: Plastid, chloroplast : Q9SR19
• Total number of polymer chains: 1
• Total formula weight: 24004.91

Authors

Hauser, T.,Bhat, J.Y.,Milicic, G.,Wendler, P.,Hartl, F.U.,Bracher, A.,Hayer-Hartl, M. (deposition date: 2014-10-29, release date: 2015-07-22, Last modification date: 2024-05-08)

Primary citation

Hauser, T.,Bhat, J.Y.,Milicic, G.,Wendler, P.,Hartl, F.U.,Bracher, A.,Hayer-Hartl, M.
Structure and mechanism of the Rubisco-assembly chaperone Raf1.
Nat.Struct.Mol.Biol., 22:720-728, 2015

PubMed Abstract: 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 ∼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 β-sheet dimerization domain and a flexibly linked α-helical domain. Chemical cross-linking and EM reconstruction indicate that the β-domains bind along the equator of each RbcL2 unit, and the α-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.

PubMed: 26237510
DOI: 10.1038/nsmb.3062

Experimental method

X-RAY DIFFRACTION (1.954 Å)