|Entry||Database: EMDB / ID: 6179|
|Title||One state of F-Actin at near-atomic resolution|
|Map data||reconstruction of F-actin|
|Sample||Skeletal muscle actin:|
|Keywords||helical polymer / actin filament|
|Function / homology||Actin, conserved site / Actin/actin-like conserved site / Actin family / Actins and actin-related proteins signature. / Actins signature 2. / Actins signature 1. / Actin / positive regulation of actin-dependent ATPase activity / mesenchyme migration / tropomyosin binding ...Actin, conserved site / Actin/actin-like conserved site / Actin family / Actins and actin-related proteins signature. / Actins signature 2. / Actins signature 1. / Actin / positive regulation of actin-dependent ATPase activity / mesenchyme migration / tropomyosin binding / myosin heavy chain binding / troponin I binding / skeletal muscle thin filament assembly / striated muscle thin filament / actin filament bundle / filamentous actin / actin filament bundle assembly / actin monomer binding / skeletal muscle fiber development / skeletal muscle myofibril / stress fiber / titin binding / actin filament polymerization / actin filament / filopodium / calcium-dependent protein binding / cell body / lamellipodium / protein domain specific binding / positive regulation of gene expression / magnesium ion binding / calcium ion binding / ATP binding / identical protein binding / cytoplasm / Actin, alpha skeletal muscle|
Function and homology information
|Source||Oryctolagus cuniculus (rabbit)|
|Method||helical reconstruction / cryo EM / 4.7 Å resolution|
|Authors||Galkin VE / Orlova A / Vos MR / Schroder GF / Egelman EH|
|Citation||Journal: Structure / Year: 2015|
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.
Copyright: 2015 Elsevier Ltd. All rights reserved.
|Validation Report||PDB-ID: 3j8i|
SummaryFull reportAbout validation report
|Date||Deposition: Nov 6, 2014 / Header (metadata) release: Dec 24, 2014 / Map release: Jan 14, 2015 / Last update: Jan 14, 2015|
|Structure viewer||EM map: |
Downloads & links
|File||emd_6179.map.gz (map file in CCP4 format, 20001 KB)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 1.05 Å|
CCP4 map header:
-Entire Skeletal muscle actin
|Entire||Name: Skeletal muscle actin / Number of components: 1 / Oligomeric State: polymer|
-Component #1: protein, actin
|Protein||Name: actin / Recombinant expression: No|
|Source||Species: Oryctolagus cuniculus (rabbit)|
|Source (natural)||Organ or tissue: skeletal muscle|
|Specimen||Specimen state: filament / Method: cryo EM|
|Helical parameters||Axial symmetry: C1 (asymmetric) / Hand: LEFT HANDED / Delta z: 27.6 Å / Delta phi: 166.7 deg.|
|Vitrification||Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 90 %|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Imaging||Microscope: FEI TITAN KRIOS / Date: Oct 9, 2014|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM|
|Lens||Cs: 2.7 mm / Imaging mode: BRIGHT FIELD / Defocus: 500 - 3000 nm|
|Specimen Holder||Model: FEI TITAN KRIOS AUTOGRID HOLDER|
|Camera||Detector: FEI FALCON II (4k x 4k)|
|Image acquisition||Number of digital images: 850|
|Processing||Method: helical reconstruction / Details: IHRSR|
|3D reconstruction||Software: EMAN2, Spider / Resolution: 4.7 Å / Resolution method: OTHER|
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