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- PDB-8xqw: Cryo-EM structure of the Ycf2-FtsHi motor complex from Chlamydomo... -
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Open data
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Basic information
Entry | Database: PDB / ID: 8xqw | |||||||||
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Title | Cryo-EM structure of the Ycf2-FtsHi motor complex from Chlamydomonas reinhardtii in AMPPNP bound state | |||||||||
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![]() | MEMBRANE PROTEIN / ATP-motor / Ycf2 / FtsHi | |||||||||
Function / homology | ![]() phytochromobilin biosynthetic process / oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor / poly(ADP-ribose) glycohydrolase / cobalt ion binding / acyl carrier activity / chloroplast / oxidoreductase activity / hydrolase activity / membrane Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.9 Å | |||||||||
![]() | Liang, K. / Zhan, X. / Wu, J. / Yan, Z. | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Conservation and specialization of the Ycf2-FtsHi chloroplast protein import motor in green algae. Authors: Ke Liang / Xiechao Zhan / Yuxin Li / Yi Yang / Yanqiu Xie / Zeyu Jin / Xiaoyan Xu / Wenwen Zhang / Yang Lu / Sheng Zhang / Yilong Zou / Shan Feng / Jianping Wu / Zhen Yan / ![]() Abstract: The protein import motor in chloroplasts plays a pivotal role in their biogenesis and homeostasis by driving the translocation of preproteins into chloroplasts. While the Ycf2-FtsHi complex serves as ...The protein import motor in chloroplasts plays a pivotal role in their biogenesis and homeostasis by driving the translocation of preproteins into chloroplasts. While the Ycf2-FtsHi complex serves as the import motor in land plants, its evolutionary conservation, specialization, and mechanisms across photosynthetic organisms are largely unexplored. Here, we isolated and determined the cryogenic electron microscopy (cryo-EM) structures of the native Ycf2-FtsHi complex from Chlamydomonas reinhardtii, uncovering a complex composed of up to 19 subunits, including multiple green-algae-specific components. The heterohexameric AAA+ ATPase motor module is tilted, potentially facilitating preprotein handover from the translocon at the inner chloroplast membrane (TIC) complex. Preprotein interacts with Ycf2-FtsHi and enhances its ATPase activity in vitro. Integrating Ycf2-FtsHi and translocon at the outer chloroplast membrane (TOC)-TIC supercomplex structures reveals insights into their physical and functional interplay during preprotein translocation. By comparing these findings with those from land plants, our study establishes a structural foundation for understanding the assembly, function, evolutionary conservation, and diversity of chloroplast protein import motors. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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PDBx/mmCIF format | ![]() | 1.7 MB | Display | ![]() |
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PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 38589MC ![]() 8xqxC C: citing same article ( M: map data used to model this data |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Components
+Protein , 21 types, 22 molecules ABCDEFGHIJKLMNOPQRSTVU
-Sugars , 1 types, 2 molecules 
#29: Sugar |
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-Non-polymers , 8 types, 21 molecules 












#22: Chemical | ChemComp-LMG / #23: Chemical | ChemComp-ANP / #24: Chemical | ChemComp-MG / | #25: Chemical | #26: Chemical | #27: Chemical | #28: Chemical | Mass: 416.723 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C29H52O #30: Chemical | |
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-Details
Has ligand of interest | N |
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Has protein modification | Y |
-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
Component | Name: The Ycf2-FtsHi motor complex from Chlamydomonas / Type: COMPLEX / Entity ID: #1-#18, #21, #20, #19 / Source: NATURAL |
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Source (natural) | Organism: ![]() ![]() |
Buffer solution | pH: 7.4 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 1400 nm |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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3D reconstruction | Resolution: 2.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 172550 / Symmetry type: POINT |
Atomic model building | Source name: Other / Type: in silico model |