7VCF
Cryo-EM structure of Chlamydomonas TOC-TIC supercomplex
Summary for 7VCF
| Entry DOI | 10.2210/pdb7vcf/pdb |
| EMDB information | 31890 |
| Descriptor | Tic214, Tic12, Unknown fragment, ... (19 entities in total) |
| Functional Keywords | complex, translocase, channel |
| Biological source | Chlamydomonas reinhardtii More |
| Total number of polymer chains | 15 |
| Total formula weight | 855697.12 |
| Authors | |
| Primary citation | Jin, 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: 36413996DOI: 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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