8ILB

The complexes of RbcL, AtRaf1 and AtBSD2 (LFB)

8ILB の概要

• エントリーDOI: 10.2210/pdb8ilb/pdb
• EMDBエントリー: 35532
• 分子名称: Ribulose bisphosphate carboxylase large chain, Rubisco accumulation factor 1.2, chloroplastic, Protein BUNDLE SHEATH DEFECTIVE 2, chloroplastic (3 entities in total)
• 機能のキーワード: rubisco assembl intermidates, complex, chaperone, lyase-chaperone complex, lyase/chaperone
• 由来する生物種: Synechococcus elongatus PCC 6301; 詳細
• タンパク質・核酸の鎖数: 18
• 化学式量合計: 574441.71

構造登録者

Wang, R.,Song, H.,Zhang, W.,Wang, N.,Zhang, S.,Shao, R. (登録日: 2023-03-03, 公開日: 2023-11-01, 最終更新日: 2023-12-20)

主引用文献

Wang, R.,Song, H.,Zhang, W.,Wang, N.,Zhang, S.,Shao, R.,Liu, C.
Structural insights into the functions of Raf1 and Bsd2 in hexadecameric Rubisco assembly.
Mol Plant, 16:1927-1936, 2023

PubMed Abstract: Hexadecameric form I Rubisco, which consisting consists of eight large (RbcL) and eight small (RbcS) subunits, is the most abundant enzyme on earth. Extensive efforts to engineer an improved Rubisco to speed up its catalytic efficiency and ultimately increase agricultural productivity. However, difficulties with correct folding and assembly in foreign hosts or in vitro have hampered the genetic manipulation of hexadecameric Rubisco. In this study, we reconstituted Synechococcus sp. PCC6301 Rubisco in vitro using the chaperonin system and assembly factors from cyanobacteria and Arabidopsis thaliana (At). Rubisco holoenzyme was produced in the presence of cyanobacterial Rubisco accumulation factor 1 (Raf1) alone or both AtRaf1 and bundle-sheath defective-2 (AtBsd2) from Arabidopsis. RbcL released from GroEL is assembly capable in the presence of ATP, and AtBsd2 functions downstream of AtRaf1. Cryo-EM structures of RbcL-AtRaf1, RbcL-AtRaf1-AtBsd2, and RbcL revealed that the interactions between RbcL and AtRaf1 are looser than those between prokaryotic RbcL and Raf1, with AtRaf1 tilting 7° farther away from RbcL. AtBsd2 stabilizes the flexible regions of RbcL, including the N and C termini, the 60s loop, and loop 6. Using these data, combined with previous findings, we propose the possible biogenesis pathways of prokaryotic and eukaryotic Rubisco.

PubMed: 37853692
DOI: 10.1016/j.molp.2023.10.011

実験手法

ELECTRON MICROSCOPY (3 Å)