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8IOL

The complex of Rubisco large subunit (RbcL)

Summary for 8IOL
Entry DOI10.2210/pdb8iol/pdb
EMDB information35621
DescriptorRibulose bisphosphate carboxylase large chain (1 entity in total)
Functional Keywordsrubisco large subunit, complex, photosynthesis, lyase
Biological sourceSynechococcus elongatus PCC 6301
Total number of polymer chains8
Total formula weight420132.84
Authors
Wang, R.,Song, H.,Zhang, W.,Wang, N.,Zhang, S.,Shao, R. (deposition date: 2023-03-11, release date: 2023-11-01, Last modification date: 2024-10-30)
Primary citationWang, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.9 Å)
Structure validation

226707

数据于2024-10-30公开中

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