7XSD

Cryo-EM structure of RuBisCO assembly intermediate RbcL8Raf18RbcX16

7XSD の概要

• エントリーDOI: 10.2210/pdb7xsd/pdb
• EMDBエントリー: 33524
• 分子名称: RuBisCO chaperone RbcX, RuBisCO accumulation factor 1, Ribulose bisphosphate carboxylase large chain (3 entities in total)
• 機能のキーワード: rubisco intermediate, photosynthesis
• 由来する生物種: Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576); 詳細
• タンパク質・核酸の鎖数: 32
• 化学式量合計: 996668.54

構造登録者

Jiang, Y.L.,Xia, L.Y.,Zhou, C.Z. (登録日: 2022-05-13, 公開日: 2022-07-06, 最終更新日: 2024-07-03)

主引用文献

Li, Q.,Jiang, Y.L.,Xia, L.Y.,Chen, Y.,Zhou, C.Z.
Structural insights into cyanobacterial RuBisCO assembly coordinated by two chaperones Raf1 and RbcX.
Cell Discov, 8:93-93, 2022

PubMed Abstract: RuBisCO is the most abundant enzyme in nature, catalyzing the fixation of CO in photosynthesis. Its common form consists of eight RbcL and eight RbcS subunits, the assembly of which requires a series of chaperones that include RbcX and RuBisCO accumulation factor 1 (Raf1). To understand how these RuBisCO-specific chaperones function during cyanobacterial RbcLRbcS (LS) holoenzyme formation, we solved a 3.3-Å cryo-electron microscopy structure of a 32-subunit RbcLRaf1RbcX (LFX) assembly intermediate from Anabaena sp. PCC 7120. Comparison to the previously resolved LF and LX structures together with biochemical assays revealed that the LFX complex forms a rather dynamic structural intermediate, favoring RbcS displacement of Raf1 and RbcX. In vitro assays further demonstrated that both Raf1 and RbcX function to regulate RuBisCO condensate formation by restricting CcmM35 binding to the stably assembled LS holoenzymes. Combined with previous findings, we propose a model on how Raf1 and RbcX work in concert to facilitate, and regulate, cyanobacterial RuBisCO assembly as well as disassembly of RuBisCO condensates.

PubMed: 36123352
DOI: 10.1038/s41421-022-00436-9

実験手法

ELECTRON MICROSCOPY (3.3 Å)