4WT3

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

4WT3 の概要

• エントリーDOI: 10.2210/pdb4wt3/pdb
• 分子名称: Rubisco Accumulation Factor 1, isoform 2 (2 entities in total)
• 機能のキーワード: assembly chaperone, chaperone
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• 細胞内の位置: Plastid, chloroplast : Q9SR19
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24004.91

構造登録者

Hauser, T.,Bhat, J.Y.,Milicic, G.,Wendler, P.,Hartl, F.U.,Bracher, A.,Hayer-Hartl, M. (登録日: 2014-10-29, 公開日: 2015-07-22, 最終更新日: 2024-05-08)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.954 Å)