+
Open data
-
Basic information
Entry | Database: PDB / ID: 3j8j | ||||||
---|---|---|---|---|---|---|---|
Title | Tilted state of actin, T1 | ||||||
![]() | Actin, alpha skeletal muscle![]() | ||||||
![]() | ![]() ![]() | ||||||
Function / homology | ![]() cytoskeletal motor activator activity / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Galkin, V.E. / Orlova, A. / Vos, M.R. / Schroder, G.F. / Egelman, E.H. | ||||||
![]() | ![]() Title: Near-atomic resolution for one state of F-actin. Authors: Vitold E Galkin / Albina Orlova / Matthijn R Vos / Gunnar F Schröder / Edward H Egelman / ![]() ![]() ![]() Abstract: Actin functions as a helical polymer, F-actin, but attempts to build an atomic model for this filament have been hampered by the fact that the filament cannot be crystallized and by structural ...Actin functions as a helical polymer, F-actin, but attempts to build an atomic model for this filament have been hampered by the fact that the filament cannot be crystallized and by structural heterogeneity. We have used a direct electron detector, cryo-electron microscopy, and the forces imposed on actin filaments in thin films to reconstruct one state of the filament at 4.7 Å resolution, which allows for building a reliable pseudo-atomic model of F-actin. We also report a different state of the filament where actin protomers adopt a conformation observed in the crystal structure of the G-actin-profilin complex with an open ATP-binding cleft. Comparison of the two structural states provides insights into ATP-hydrolysis and filament dynamics. The atomic model provides a framework for understanding why every buried residue in actin has been under intense selective pressure. | ||||||
History |
|
-
Structure visualization
Movie |
![]() |
---|---|
Structure viewer | Molecule: ![]() ![]() |
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 689.6 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 586 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
---|
-Related structure data
Related structure data | ![]() 6180MC ![]() 6179C ![]() 6181C ![]() 3j8iC ![]() 3j8kC M: map data used to model this data C: citing same article ( |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
|
---|---|
1 |
|
Symmetry | Helical symmetry: (Circular symmetry: 1 / Dyad axis: no / N subunits divisor: 1 / Num. of operations: 11 / Rise per n subunits: 28.3 Å / Rotation per n subunits: -166.8 °) |
Details | Actin forms a helical filament of indeterminate length. The designation "undecameric" in REMARK 350 is an artifact of the PDB format and can be disregarded. |
-
Components
#1: Protein | ![]() Mass: 42096.953 Da / Num. of mol.: 11 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() ![]() ![]() |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|---|
EM experiment | Aggregation state: FILAMENT / 3D reconstruction method: helical reconstruction |
-
Sample preparation
Component | Name: Skeletal muscle actin / Type: COMPLEX / Details: polymer |
---|---|
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied![]() ![]() |
Vitrification![]() | Instrument: HOMEMADE PLUNGER / Cryogen name: ETHANE / Humidity: 90 % / Details: Plunged into liquid ethane |
-
Electron microscopy imaging
Experimental equipment | ![]() Model: Tecnai F20 / Image courtesy: FEI Company |
---|---|
Microscopy | Model: FEI TECNAI F20 / Date: Oct 9, 2014 |
Electron gun | Electron source![]() ![]() |
Electron lens | Mode: BRIGHT FIELD![]() ![]() |
Specimen holder | Specimen holder model: GATAN LIQUID NITROGEN |
Image recording | Film or detector model: KODAK SO-163 FILM |
Image scans | Num. digital images: 437 |
-
Processing
EM software |
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Helical symmerty | Angular rotation/subunit: 166.8 ° / Axial rise/subunit: 28.3 Å / Axial symmetry: C1 | ||||||||||||
3D reconstruction![]() | Resolution: 12 Å / Resolution method: FSC / Nominal pixel size: 2.5 Å / Actual pixel size: 2.5 Å / Details: (Helical Details: IHRSR) / Symmetry type: HELICAL | ||||||||||||
Refinement step | Cycle: LAST
|