+
Open data
-
Basic information
Entry | Database: PDB / ID: 7ajc | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | bovine ATP synthase dimer state1:state2 | |||||||||
![]() |
| |||||||||
![]() | HYDROLASE / ATP synthase / mitochondria / mammalian / complex | |||||||||
Function / homology | ![]() angiostatin binding / Formation of ATP by chemiosmotic coupling / Cristae formation / ATPase inhibitor activity / mitochondrial proton-transporting ATP synthase complex assembly / mitochondrial envelope / negative regulation of hydrolase activity / proton-transporting ATP synthase complex / heme biosynthetic process / : ...angiostatin binding / Formation of ATP by chemiosmotic coupling / Cristae formation / ATPase inhibitor activity / mitochondrial proton-transporting ATP synthase complex assembly / mitochondrial envelope / negative regulation of hydrolase activity / proton-transporting ATP synthase complex / heme biosynthetic process / : / : / : / : / Mitochondrial protein degradation / proton-transporting ATP synthase complex, coupling factor F(o) / : / negative regulation of endothelial cell proliferation / proton transmembrane transporter activity / proton motive force-driven ATP synthesis / proton motive force-driven mitochondrial ATP synthesis / proton-transporting ATP synthase complex, catalytic core F(1) / H+-transporting two-sector ATPase / aerobic respiration / proton-transporting ATPase activity, rotational mechanism / proton transmembrane transport / proton-transporting ATP synthase activity, rotational mechanism / erythrocyte differentiation / ADP binding / ATPase binding / protein homotetramerization / mitochondrial inner membrane / calmodulin binding / lipid binding / structural molecule activity / cell surface / protein homodimerization activity / ATP hydrolysis activity / protein-containing complex / mitochondrion / ATP binding / identical protein binding / plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 11.9 Å | |||||||||
![]() | Spikes, T.E. / Montgomery, M.G. / Walker, J.E. | |||||||||
Funding support | ![]()
| |||||||||
![]() | ![]() Title: Interface mobility between monomers in dimeric bovine ATP synthase participates in the ultrastructure of inner mitochondrial membranes. Authors: Tobias E Spikes / Martin G Montgomery / John E Walker / ![]() Abstract: The ATP synthase complexes in mitochondria make the ATP required to sustain life by a rotary mechanism. Their membrane domains are embedded in the inner membranes of the organelle, and they dimerize ...The ATP synthase complexes in mitochondria make the ATP required to sustain life by a rotary mechanism. Their membrane domains are embedded in the inner membranes of the organelle, and they dimerize via interactions between their membrane domains. The dimers form extensive chains along the tips of the cristae with the two rows of monomeric catalytic domains extending into the mitochondrial matrix at an angle to each other. Disruption of the interface between dimers by mutation affects the morphology of the cristae severely. By analysis of particles of purified dimeric bovine ATP synthase by cryo-electron microscopy, we have shown that the angle between the central rotatory axes of the monomeric complexes varies between ca. 76 and 95°. These particles represent active dimeric ATP synthase. Some angular variations arise directly from the catalytic mechanism of the enzyme, and others are independent of catalysis. The monomer-monomer interaction is mediated mainly by j subunits attached to the surface of wedge-shaped protein-lipid structures in the membrane domain of the complex, and the angular variation arises from rotational and translational changes in this interaction, and combinations of both. The structures also suggest how the dimeric ATP synthases might be interacting with each other to form the characteristic rows along the tips of the cristae via other interwedge contacts, molding themselves to the range of oligomeric arrangements observed by tomography of mitochondrial membranes, and at the same time allowing the ATP synthase to operate under the range of physiological conditions that influence the structure of the cristae. | |||||||||
History |
|
-
Structure visualization
Movie |
![]() |
---|---|
Structure viewer | Molecule: ![]() ![]() |
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 1.3 MB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
---|
-Related structure data
Related structure data | ![]() 11429MC ![]() 7ajbC ![]() 7ajdC ![]() 7ajeC ![]() 7ajfC ![]() 7ajgC ![]() 7ajhC ![]() 7ajiC ![]() 7ajjC M: map data used to model this data C: citing same article ( |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
|
---|---|
1 |
|
-
Components
-ATP synthase ... , 16 types, 54 molecules 8A8ABCAAABACDEFADAEAFGAGHAHIAIKLMNOPQRAKAL...
#1: Protein | Mass: 7944.523 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #2: Protein | Mass: 55302.191 Da / Num. of mol.: 6 / Source method: isolated from a natural source Details: Residue 1 of chains A, B, C. The uniprot database is misleading stating that GLN is the first residue. The DNA sequence for this protein encodes GLU. The actual residue is pyroGLU. However ...Details: Residue 1 of chains A, B, C. The uniprot database is misleading stating that GLN is the first residue. The DNA sequence for this protein encodes GLU. The actual residue is pyroGLU. However pyroGLU and pyroGLN are the same. Residue 481 in chains A, B, and C can be Gly or SER. e.g. in this structure should be GLY. We have seen SER in some of our previous structures of bovine F1-ATPase. We have used the following REMARK in other PDB files: Microhetrogeneity REMARK 999 SER 481 GLY IN CHAINS A, B AND C REMARK 999 WAS IDENTIFIED AS A GLY FROM THE PROTEIN REMARK 999 SEQUENCE. IN THE CDNA SEQUENCE, THE CODON FOR THIS REMARK 999 RESIDUE WAS AGC SER IN THREE CLONES WHILE IN TWO REMARK 999 OTHERS IT WAS GGC GLY. THE DIFFERENCE WAS THOUGHT TO REMARK 999 BE DUE TO A MUTATION OCCURRING DURING EITHER PROPAGATION REMARK 999 OF THE CLONES IN THE LIBRARY OR SUBCLONING INTO M13 REMARK 999 VECTORS. THE ELECTRON DENSITY SUGGESTS A GLY IN REMARK 999 THIS POSITION. Source: (natural) ![]() ![]() #3: Protein | Mass: 51757.836 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() References: UniProt: P00829, H+-transporting two-sector ATPase #4: Protein | Mass: 30300.760 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #5: Protein | Mass: 15074.813 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #6: Protein/peptide | Mass: 5662.693 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #8: Protein | Mass: 7653.034 Da / Num. of mol.: 16 / Source method: isolated from a natural source Details: Uniprot P07926. The cross reference box is not working. Source: (natural) ![]() ![]() #9: Protein | Mass: 20959.777 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: Uniprot p13621. The cross ref box isn't working / Source: (natural) ![]() ![]() #10: Protein | Mass: 24801.785 Da / Num. of mol.: 2 / Source method: isolated from a natural source Details: Uniprot P00847. The cross reference gui box isn't working. Source: (natural) ![]() ![]() #11: Protein | Mass: 24702.709 Da / Num. of mol.: 2 / Source method: isolated from a natural source Details: Uniprot P13619. The cross reference gui is not working. Source: (natural) ![]() ![]() #12: Protein | Mass: 18588.256 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: Uniprot P13620. The cross-ref gui isn't working / Source: (natural) ![]() ![]() #13: Protein | Mass: 8205.492 Da / Num. of mol.: 2 / Source method: isolated from a natural source Details: Uniprot Q00361. The cross reference gui isn't working. Source: (natural) ![]() ![]() #14: Protein | Mass: 10184.011 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: Uniprot Q28851. The cross ref gui isn't working / Source: (natural) ![]() ![]() #15: Protein | Mass: 11298.196 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: Uniprot Q28852. The cross ref gui isn't working / Source: (natural) ![]() ![]() #17: Protein | Mass: 6846.093 Da / Num. of mol.: 2 / Source method: isolated from a natural source Details: uniprot P14790. The cross reference gui isn't working. Source: (natural) ![]() ![]() #18: Protein | Mass: 6312.383 Da / Num. of mol.: 2 / Source method: isolated from a natural source Details: Uniprot Q3ZBI7. The cross reference gui isn't working. Source: (natural) ![]() ![]() |
---|
-Protein , 2 types, 4 molecules JAJhAh
#7: Protein | Mass: 7462.098 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: residues 1-60 with a 6 his tag / Source: (gene. exp.) ![]() ![]() ![]() ![]() #16: Protein | Mass: 8971.079 Da / Num. of mol.: 2 / Source method: isolated from a natural source Details: Uniprot P02721. The Cross reference gui isn't working. Source: (natural) ![]() ![]() |
---|
-Non-polymers , 2 types, 10 molecules ![](data/chem/img/CDL.gif)
![](data/chem/img/LHG.gif)
![](data/chem/img/LHG.gif)
#19: Chemical | ChemComp-CDL / #20: Chemical | ChemComp-LHG / |
---|
-Details
Has ligand of interest | N |
---|
-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
---|---|
EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-
Sample preparation
Component |
| ||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Molecular weight | Value: 1.18 MDa / Experimental value: YES | ||||||||||||||||||||||||
Source (natural) |
| ||||||||||||||||||||||||
Source (recombinant) | Organism: ![]() ![]() | ||||||||||||||||||||||||
Buffer solution | pH: 7.4 | ||||||||||||||||||||||||
Specimen | Conc.: 4.5 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||
Specimen support | Grid material: GOLD / Grid type: UltrAuFoil | ||||||||||||||||||||||||
Vitrification | Cryogen name: ETHANE |
-
Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
---|---|
Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD |
Image recording | Electron dose: 55 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 QUANTUM (4k x 4k) |