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7VCF

Cryo-EM structure of Chlamydomonas TOC-TIC supercomplex

Summary for 7VCF
Entry DOI10.2210/pdb7vcf/pdb
EMDB information31890
DescriptorTic214, Tic12, Unknown fragment, ... (19 entities in total)
Functional Keywordscomplex, translocase, channel
Biological sourceChlamydomonas reinhardtii
More
Total number of polymer chains15
Total formula weight855697.12
Authors
Wu, J.,Yan, Z.,Jin, Z.,Zhang, Y. (deposition date: 2021-09-02, release date: 2022-11-30, Last modification date: 2025-07-02)
Primary citationJin, Z.,Wan, L.,Zhang, Y.,Li, X.,Cao, Y.,Liu, H.,Fan, S.,Cao, D.,Wang, Z.,Li, X.,Pan, J.,Dong, M.Q.,Wu, J.,Yan, Z.
Structure of a TOC-TIC supercomplex spanning two chloroplast envelope membranes.
Cell, 185:4788-4800.e13, 2022
Cited by
PubMed Abstract: The TOC and TIC complexes are essential translocons that facilitate the import of the nuclear genome-encoded preproteins across the two envelope membranes of chloroplast, but their exact molecular identities and assembly remain unclear. Here, we report a cryoelectron microscopy structure of TOC-TIC supercomplex from Chlamydomonas, containing a total of 14 identified components. The preprotein-conducting pore of TOC is a hybrid β-barrel co-assembled by Toc120 and Toc75, while the potential translocation path of TIC is formed by transmembrane helices from Tic20 and YlmG, rather than a classic model of Tic110. A rigid intermembrane space (IMS) scaffold bridges two chloroplast membranes, and a large hydrophilic cleft on the IMS scaffold connects TOC and TIC, forming a pathway for preprotein translocation. Our study provides structural insights into the TOC-TIC supercomplex composition, assembly, and preprotein translocation mechanism, and lays a foundation to interpret the evolutionary conservation and diversity of this fundamental translocon machinery.
PubMed: 36413996
DOI: 10.1016/j.cell.2022.10.030
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.5 Å)
Structure validation

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