8XKS
The cryo-EM structure of Orf2971-FtsHi motor complex
Summary for 8XKS
| Entry DOI | 10.2210/pdb8xks/pdb |
| EMDB information | 38424 |
| Descriptor | Ctap1, Fatty acid desaturase domain-containing protein, Moc25, ... (25 entities in total) |
| Functional Keywords | chlamydomonas reinhardtii, protein transportation, chloroplast, lipid synthesis, enzyme, protein transport |
| Biological source | Chlamydomonas reinhardtii (Chlamydomonas smithii) More |
| Total number of polymer chains | 20 |
| Total formula weight | 1509080.90 |
| Authors | |
| Primary citation | Wang, N.,Xing, J.,Su, X.,Pan, J.,Chen, H.,Shi, L.,Si, L.,Yang, W.,Li, M. Architecture of the ATP-driven motor for protein import into chloroplasts. Mol Plant, 17:1702-1718, 2024 Cited by PubMed Abstract: Thousands of nuclear-encoded proteins are transported into chloroplasts through the TOC-TIC translocon that spans the chloroplast envelope membranes. A motor complex pulls the translocated proteins out of the TOC-TIC complex into the chloroplast stroma by hydrolyzing ATP. The Orf2971-FtsHi complex has been suggested to serve as the ATP-hydrolyzing motor in Chlamydomonas reinhardtii, but little is known about its architecture and assembly. Here, we report the 3.2-Å resolution structure of the Chlamydomonas Orf2971-FtsHi complex. The 20-subunit complex spans the chloroplast inner envelope, with two bulky modules protruding into the intermembrane space and stromal matrix. Six subunits form a hetero-hexamer that potentially provides the pulling force through ATP hydrolysis. The remaining subunits, including potential enzymes/chaperones, likely facilitate the complex assembly and regulate its proper function. Taken together, our results provide the structural foundation for a mechanistic understanding of chloroplast protein translocation. PubMed: 39327731DOI: 10.1016/j.molp.2024.09.010 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.2 Å) |
Structure validation
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