6FKF

Chloroplast F1Fo conformation 1


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.15 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Structure, mechanism, and regulation of the chloroplast ATP synthase.

Hahn, A.Vonck, J.Mills, D.J.Meier, T.Kuhlbrandt, W.

(2018) Science 360

  • DOI: https://doi.org/10.1126/science.aat4318
  • Primary Citation of Related Structures:  
    6FKF, 6FKH, 6FKI

  • PubMed Abstract: 

    The chloroplast adenosine triphosphate (ATP) synthase uses the electrochemical proton gradient generated by photosynthesis to produce ATP, the energy currency of all cells. Protons conducted through the membrane-embedded F o motor drive ATP synthesis in the F 1 head by rotary catalysis. We determined the high-resolution structure of the complete cF 1 F o complex by cryo-electron microscopy, resolving side chains of all 26 protein subunits, the five nucleotides in the F 1 head, and the proton pathway to and from the rotor ring. The flexible peripheral stalk redistributes differences in torsional energy across three unequal steps in the rotation cycle. Plant ATP synthase is autoinhibited by a β-hairpin redox switch in subunit γ that blocks rotation in the dark.


  • Organizational Affiliation

    Department of Structural Biology, Max Planck Institute of Biophysics, Max-von-Laue-Strasse 3, 60438 Frankfurt am Main, Germany.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
ATP synthase subunit alpha, chloroplastic
A, C, E
507Spinacia oleraceaMutation(s): 0 
EC: 3.6.3.14
Membrane Entity: Yes 
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UniProt GroupP06450
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
ATP synthase subunit beta, chloroplastic
B, D, F
498Spinacia oleraceaMutation(s): 0 
EC: 3.6.3.14
Membrane Entity: Yes 
UniProt
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
ATP synthase gamma chain, chloroplasticG [auth g]364Spinacia oleraceaMutation(s): 0 
Membrane Entity: Yes 
UniProt
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
ATP synthase delta chain, chloroplasticH [auth d]257Spinacia oleraceaMutation(s): 0 
Membrane Entity: Yes 
UniProt
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UniProt GroupP11402
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Entity ID: 5
MoleculeChains Sequence LengthOrganismDetailsImage
ATP synthase subunit b', chloroplasticI [auth p]222Spinacia oleraceaMutation(s): 0 
Membrane Entity: Yes 
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Entity ID: 6
MoleculeChains Sequence LengthOrganismDetailsImage
ATP synthase subunit b, chloroplasticJ [auth b]184Spinacia oleraceaMutation(s): 0 
Membrane Entity: Yes 
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Entity ID: 7
MoleculeChains Sequence LengthOrganismDetailsImage
ATP synthase subunit a, chloroplasticK [auth a]247Spinacia oleraceaMutation(s): 0 
Membrane Entity: Yes 
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Entity ID: 8
MoleculeChains Sequence LengthOrganismDetailsImage
ATP synthase subunit c, chloroplastic81Spinacia oleraceaMutation(s): 0 
Membrane Entity: Yes 
UniProt
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Entity ID: 9
MoleculeChains Sequence LengthOrganismDetailsImage
ATP synthase epsilon chain, chloroplasticZ [auth e]134Spinacia oleraceaMutation(s): 0 
Membrane Entity: Yes 
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Small Molecules
Ligands 3 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
ATP
Query on ATP

Download Ideal Coordinates CCD File 
AA [auth A],
CA [auth C],
GA [auth E]
ADENOSINE-5'-TRIPHOSPHATE
C10 H16 N5 O13 P3
ZKHQWZAMYRWXGA-KQYNXXCUSA-N
ADP
Query on ADP

Download Ideal Coordinates CCD File 
EA [auth D],
IA [auth F]
ADENOSINE-5'-DIPHOSPHATE
C10 H15 N5 O10 P2
XTWYTFMLZFPYCI-KQYNXXCUSA-N
MG
Query on MG

Download Ideal Coordinates CCD File 
BA [auth A],
DA [auth C],
FA [auth D],
HA [auth E],
JA [auth F]
MAGNESIUM ION
Mg
JLVVSXFLKOJNIY-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.15 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 
EM Software:
TaskSoftware PackageVersion
MODEL REFINEMENTPHENIX
RECONSTRUCTIONRELION2.1

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2018-05-23
    Type: Initial release
  • Version 1.1: 2018-06-06
    Changes: Advisory, Data collection, Derived calculations
  • Version 1.2: 2018-10-17
    Changes: Data collection, Refinement description
  • Version 1.3: 2019-12-11
    Changes: Other