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- EMDB-38589: Cryo-EM structure of the Ycf2-FtsHi motor complex from Chlamydomo... -
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Open data
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Basic information
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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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![]() | ATP-motor / Ycf2 / FtsHi / MEMBRANE PROTEIN | |||||||||
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 | 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
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 168.2 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 46.6 KB 46.6 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 11.8 KB | Display | ![]() |
Images | ![]() | 72.7 KB | ||
Filedesc metadata | ![]() | 15.1 KB | ||
Others | ![]() ![]() | 165.3 MB 165.3 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8xqwMC ![]() 8xqxC C: citing same article ( M: atomic model generated by this map |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.087 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_38589_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_38589_half_map_2.map | ||||||||||||
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Density Histograms |
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Sample components
+Entire : The Ycf2-FtsHi motor complex from Chlamydomonas
+Supramolecule #1: The Ycf2-FtsHi motor complex from Chlamydomonas
+Macromolecule #1: Fhl1
+Macromolecule #2: Fhl3
+Macromolecule #3: Ycf2
+Macromolecule #4: Ctap1
+Macromolecule #5: Ctap6
+Macromolecule #6: ARHL
+Macromolecule #7: PcyA
+Macromolecule #8: CrTam39
+Macromolecule #9: ACP
+Macromolecule #10: CrTam29
+Macromolecule #11: CrTam34
+Macromolecule #12: FADL
+Macromolecule #13: CrTam15
+Macromolecule #14: CrTam49
+Macromolecule #15: Ctap7
+Macromolecule #16: Tic22
+Macromolecule #17: DnaJ
+Macromolecule #18: CrTam35
+Macromolecule #19: CrTam31
+Macromolecule #20: UNK
+Macromolecule #21: UNK
+Macromolecule #22: 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE
+Macromolecule #23: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
+Macromolecule #24: MAGNESIUM ION
+Macromolecule #25: 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-GLUCOPYRANOSYL]-SN-GLYCEROL
+Macromolecule #26: DIACYL GLYCEROL
+Macromolecule #27: CHOLESTEROL HEMISUCCINATE
+Macromolecule #28: Beta-Sitosterol
+Macromolecule #29: DIGALACTOSYL DIACYL GLYCEROL (DGDG)
+Macromolecule #30: ZINC ION
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.4 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.4000000000000001 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
Initial model | Chain - Source name: Other / Chain - Initial model type: in silico model |
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Output model | ![]() PDB-8xqw: |