8XKU

Cryo-EM structure of the Ycf2-FtsHi motor complex from Arabidopsis in ATP-bound state


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.20 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

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Literature

Structural insights into the chloroplast protein import in land plants.

Liang, K.Jin, Z.Zhan, X.Li, Y.Xu, Q.Xie, Y.Yang, Y.Wang, S.Wu, J.Yan, Z.

(2024) Cell 

  • DOI: https://doi.org/10.1016/j.cell.2024.08.003
  • Primary Citation of Related Structures:  
    8XKU, 8XKV

  • PubMed Abstract: 

    Chloroplast proteins are imported via the translocon at the outer chloroplast membrane (TOC)-translocon at the inner chloroplast membrane (TIC) supercomplex, driven by an ATPase motor. The Ycf2-FtsHi complex has been identified as the chloroplast import motor. However, its assembly and cooperation with the TIC complex during preprotein translocation remain unclear. Here, we present the structures of the Ycf2-FtsHi and TIC complexes from Arabidopsis and an ultracomplex formed between them from Pisum. The Ycf2-FtsHi structure reveals a heterohexameric AAA+ ATPase motor module with characteristic features. Four previously uncharacterized components of Ycf2-FtsHi were identified, which aid in complex assembly and anchoring of the motor module at a tilted angle relative to the membrane. When considering the structures of the TIC complex and the TIC-Ycf2-FtsHi ultracomplex together, it becomes evident that the tilted motor module of Ycf2-FtsHi enables its close contact with the TIC complex, thereby facilitating efficient preprotein translocation. Our study provides valuable structural insights into the chloroplast protein import process in land plants.


  • Organizational Affiliation

    Key Laboratory of Structural Biology of Zhejiang Province, School of Life Sciences, Westlake University, Hangzhou, Zhejiang 310024, China; Westlake Laboratory of Life Sciences and Biomedicine, Hangzhou, Zhejiang 310024, China; Institute of Biology, Westlake Institute for Advanced Study, Hangzhou, Zhejiang 310024, China.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Probable inactive ATP-dependent zinc metalloprotease FTSHI 4, chloroplastic855Arabidopsis thalianaMutation(s): 0 
UniProt
Find proteins for F4KF14 (Arabidopsis thaliana)
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
ATP-dependent zinc metalloprotease FTSH 12, chloroplastic1,008Arabidopsis thalianaMutation(s): 0 
EC: 3.4.24
UniProt
Find proteins for Q9SAJ3 (Arabidopsis thaliana)
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Probable inactive ATP-dependent zinc metalloprotease FTSHI 5, chloroplastic1,320Arabidopsis thalianaMutation(s): 0 
UniProt
Find proteins for F4J3N2 (Arabidopsis thaliana)
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
Protein Ycf22,294Arabidopsis thalianaMutation(s): 0 
UniProt
Find proteins for P56786 (Arabidopsis thaliana)
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Entity ID: 5
MoleculeChains Sequence LengthOrganismDetailsImage
Probable inactive ATP-dependent zinc metalloprotease FTSHI 1, chloroplastic946Arabidopsis thalianaMutation(s): 0 
UniProt
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Entity ID: 6
MoleculeChains Sequence LengthOrganismDetailsImage
Probable inactive ATP-dependent zinc metalloprotease FTSHI 2, chloroplastic876Arabidopsis thalianaMutation(s): 0 
UniProt
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Entity ID: 7
MoleculeChains Sequence LengthOrganismDetailsImage
AtTam46396Arabidopsis thalianaMutation(s): 0 
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Entity ID: 8
MoleculeChains Sequence LengthOrganismDetailsImage
At4g28210348Arabidopsis thalianaMutation(s): 0 
UniProt
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Entity ID: 9
MoleculeChains Sequence LengthOrganismDetailsImage
Malate dehydrogenase, chloroplastic
I, J
403Arabidopsis thalianaMutation(s): 0 
EC: 1.1.1.37
UniProt
Find proteins for Q9SN86 (Arabidopsis thaliana)
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Entity ID: 10
MoleculeChains Sequence LengthOrganismDetailsImage
Aspartyl/glutamyl-tRNA (Asn/Gln) amidotransferase subunit B80Arabidopsis thalianaMutation(s): 0 
UniProt
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Entity ID: 11
MoleculeChains Sequence LengthOrganismDetailsImage
UNK18Arabidopsis thalianaMutation(s): 0 
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Entity ID: 12
MoleculeChains Sequence LengthOrganismDetailsImage
UNK11Arabidopsis thalianaMutation(s): 0 
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Entity ID: 13
MoleculeChains Sequence LengthOrganismDetailsImage
UNK37Arabidopsis thalianaMutation(s): 0 
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Entity ID: 14
MoleculeChains Sequence LengthOrganismDetailsImage
UNK17Arabidopsis thalianaMutation(s): 0 
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Entity ID: 15
MoleculeChains Sequence LengthOrganismDetailsImage
UNK19Arabidopsis thalianaMutation(s): 0 
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Entity ID: 16
MoleculeChains Sequence LengthOrganismDetailsImage
Embryo defective 2737Q [auth R]328Arabidopsis thalianaMutation(s): 0 
UniProt
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Small Molecules
Ligands 4 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
PX2
Query on PX2

Download Ideal Coordinates CCD File 
W [auth B]1,2-DILAUROYL-SN-GLYCERO-3-PHOSPHATE
C27 H52 O8 P
OKLASJZQBDJAPH-RUZDIDTESA-M
ATP
Query on ATP

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S [auth A],
V [auth B]
ADENOSINE-5'-TRIPHOSPHATE
C10 H16 N5 O13 P3
ZKHQWZAMYRWXGA-KQYNXXCUSA-N
ZN
Query on ZN

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U [auth B],
X [auth R],
Y [auth R]
ZINC ION
Zn
PTFCDOFLOPIGGS-UHFFFAOYSA-N
MG
Query on MG

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R [auth A],
T [auth B]
MAGNESIUM ION
Mg
JLVVSXFLKOJNIY-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.20 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

Structure Validation

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Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
National Natural Science Foundation of China (NSFC)China32271239

Revision History  (Full details and data files)

  • Version 1.0: 2024-09-11
    Type: Initial release