+
Open data
-
Basic information
Entry | Database: EMDB / ID: EMD-5170 | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | Binding of alpha-actinin CH1 to F-actin | |||||||||
![]() | reconstructed volume of F-actin decorated with alpha-actinin ABD (CH1 and CH2) | |||||||||
![]() |
| |||||||||
![]() | helical filaments / calponin homology domains | |||||||||
Function / homology | ![]() positive regulation of glucose catabolic process to lactate via pyruvate / negative regulation of relaxation of muscle / regulation of the force of skeletal muscle contraction / skeletal muscle atrophy / positive regulation of skeletal muscle fiber development / positive regulation of norepinephrine uptake / cellular response to cytochalasin B / positive regulation of skeletal muscle tissue growth / response to denervation involved in regulation of muscle adaptation / regulation of transepithelial transport ...positive regulation of glucose catabolic process to lactate via pyruvate / negative regulation of relaxation of muscle / regulation of the force of skeletal muscle contraction / skeletal muscle atrophy / positive regulation of skeletal muscle fiber development / positive regulation of norepinephrine uptake / cellular response to cytochalasin B / positive regulation of skeletal muscle tissue growth / response to denervation involved in regulation of muscle adaptation / regulation of transepithelial transport / positive regulation of fast-twitch skeletal muscle fiber contraction / morphogenesis of a polarized epithelium / bBAF complex / postsynaptic actin cytoskeleton organization / protein localization to adherens junction / postsynaptic actin cytoskeleton / npBAF complex / Tat protein binding / brahma complex / structural constituent of postsynaptic actin cytoskeleton / nBAF complex / GBAF complex / regulation of G0 to G1 transition / dense body / Formation of annular gap junctions / transition between fast and slow fiber / positive regulation of bone mineralization involved in bone maturation / Gap junction degradation / Cell-extracellular matrix interactions / Folding of actin by CCT/TriC / apical protein localization / regulation of double-strand break repair / muscle cell development / regulation of nucleotide-excision repair / adherens junction assembly / Prefoldin mediated transfer of substrate to CCT/TriC / RSC-type complex / RHOF GTPase cycle / negative regulation of oxidative phosphorylation / focal adhesion assembly / Adherens junctions interactions / tight junction / Striated Muscle Contraction / bone morphogenesis / Sensory processing of sound by outer hair cells of the cochlea / regulation of norepinephrine uptake / negative regulation of glycolytic process / regulation of mitotic metaphase/anaphase transition / Interaction between L1 and Ankyrins / Sensory processing of sound by inner hair cells of the cochlea / Nephrin family interactions / negative regulation of cold-induced thermogenesis / SWI/SNF complex / positive regulation of double-strand break repair / regulation of synaptic vesicle endocytosis / positive regulation of T cell differentiation / negative regulation of calcineurin-NFAT signaling cascade / structural constituent of muscle / apical junction complex / regulation of aerobic respiration / establishment or maintenance of cell polarity / cortical actin cytoskeleton / regulation of cyclin-dependent protein serine/threonine kinase activity / cortical cytoskeleton / maintenance of blood-brain barrier / positive regulation of stem cell population maintenance / NuA4 histone acetyltransferase complex / nitric-oxide synthase binding / pseudopodium / Recycling pathway of L1 / regulation of G1/S transition of mitotic cell cycle / kinesin binding / brush border / calyx of Held / negative regulation of cell differentiation / positive regulation of double-strand break repair via homologous recombination / EPH-ephrin mediated repulsion of cells / RHO GTPases Activate WASPs and WAVEs / RHO GTPases activate IQGAPs / regulation of protein localization to plasma membrane / positive regulation of myoblast differentiation / EPHB-mediated forward signaling / substantia nigra development / axonogenesis / negative regulation of protein binding / cell projection / Translocation of SLC2A4 (GLUT4) to the plasma membrane / RHO GTPases Activate Formins / cell motility / actin filament / positive regulation of cell differentiation / regulation of transmembrane transporter activity / adherens junction / FCGR3A-mediated phagocytosis / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / DNA Damage Recognition in GG-NER / Signaling by high-kinase activity BRAF mutants / Schaffer collateral - CA1 synapse / MAP2K and MAPK activation / tau protein binding Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | helical reconstruction / cryo EM / Resolution: 15.0 Å | |||||||||
![]() | Galkin VE / Orlova A / Salmazo A / Djinovic-Carugo K / Egelman EH | |||||||||
![]() | ![]() Title: Opening of tandem calponin homology domains regulates their affinity for F-actin. Authors: Vitold E Galkin / Albina Orlova / Anita Salmazo / Kristina Djinovic-Carugo / Edward H Egelman / ![]() Abstract: Many actin-binding proteins contain calponin homology (CH) domains, but the manner in which these domains interact with F-actin has been controversial. Crystal structures have shown the tandem CH ...Many actin-binding proteins contain calponin homology (CH) domains, but the manner in which these domains interact with F-actin has been controversial. Crystal structures have shown the tandem CH domains of alpha-actinin to be in a compact, closed conformation, but the interpretations of complexes of such tandem CH domains with F-actin have been ambiguous. We show that the tandem CH domains of alpha-actinin bind F-actin in an open conformation, explaining mutations that cause human diseases and suggesting that the opening of these domains may be one of the main regulatory mechanisms for proteins with tandem CH domains. | |||||||||
History |
|
-
Structure visualization
Movie |
![]() |
---|---|
Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
-
Downloads & links
-EMDB archive
Map data | ![]() | 3.5 MB | ![]() | |
---|---|---|---|---|
Header (meta data) | ![]() ![]() | 8.7 KB 8.7 KB | Display Display | ![]() |
Images | ![]() | 62.3 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 310.3 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 309.8 KB | Display | |
Data in XML | ![]() | 5.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3lueMC M: atomic model generated by this map C: citing same article ( |
---|---|
Similar structure data |
-
Links
EMDB pages | ![]() ![]() |
---|---|
Related items in Molecule of the Month |
-
Map
File | ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Annotation | reconstructed volume of F-actin decorated with alpha-actinin ABD (CH1 and CH2) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 2.38 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
|
-Supplemental data
-
Sample components
-Entire : F-actin decorated with alpha-actinin ABD (containing CH1 and CH2)
Entire | Name: F-actin decorated with alpha-actinin ABD (containing CH1 and CH2) |
---|---|
Components |
|
-Supramolecule #1000: F-actin decorated with alpha-actinin ABD (containing CH1 and CH2)
Supramolecule | Name: F-actin decorated with alpha-actinin ABD (containing CH1 and CH2) type: sample / ID: 1000 / Details: none / Oligomeric state: one to one binding / Number unique components: 2 |
---|
-Macromolecule #1: F-actin
Macromolecule | Name: F-actin / type: protein_or_peptide / ID: 1 / Name.synonym: F-actin / Oligomeric state: helical polymer / Recombinant expression: Yes |
---|---|
Source (natural) | Organism: ![]() |
Recombinant expression | Organism: ![]() ![]() |
Sequence | GO: actin filament binding |
-Experimental details
-Structure determination
Method | cryo EM |
---|---|
![]() | helical reconstruction |
Aggregation state | filament |
-
Sample preparation
Vitrification | Cryogen name: ETHANE / Instrument: OTHER |
---|
-
Electron microscopy
Microscope | FEI TECNAI F20 |
---|---|
Image recording | Category: FILM / Film or detector model: KODAK SO-163 FILM / Digitization - Scanner: NIKON COOLSCAN / Digitization - Sampling interval: 12.7 µm / Bits/pixel: 16 |
Electron beam | Acceleration voltage: 200 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal magnification: 50000 |
Sample stage | Specimen holder: Gatan 626 / Specimen holder model: GATAN LIQUID NITROGEN |
Experimental equipment | ![]() Model: Tecnai F20 / Image courtesy: FEI Company |
-
Image processing
Final reconstruction | Applied symmetry - Helical parameters - Δz: 27.7 Å Applied symmetry - Helical parameters - Δ&Phi: 166.8 ° Algorithm: OTHER / Resolution.type: BY AUTHOR / Resolution: 15.0 Å / Resolution method: FSC 0.5 CUT-OFF / Software - Name: IHRSR |
---|