[English] 日本語
Yorodumi- PDB-6nbw: Ternary Complex of Beta/Gamma-Actin with Profilin and AnCoA-NAA80 -
+Open data
-Basic information
Entry | Database: PDB / ID: 6nbw | ||||||
---|---|---|---|---|---|---|---|
Title | Ternary Complex of Beta/Gamma-Actin with Profilin and AnCoA-NAA80 | ||||||
Components |
| ||||||
Keywords | STRUCTURAL PROTEIN/TRANSFERASE / acetylation / NAA80 / CYTOSOLIC PROTEIN / STRUCTURAL PROTEIN-TRANSFERASE complex | ||||||
Function / homology | Function and homology information N-terminal peptidyl-aspartic acid acetylation / N-terminal peptidyl-glutamic acid acetylation / actin modification / positive regulation of norepinephrine uptake / cellular response to cytochalasin B / regulation of actin polymerization or depolymerization / synapse maturation / peptide alpha-N-acetyltransferase activity / acetyl-CoA binding / modification of postsynaptic actin cytoskeleton ...N-terminal peptidyl-aspartic acid acetylation / N-terminal peptidyl-glutamic acid acetylation / actin modification / positive regulation of norepinephrine uptake / cellular response to cytochalasin B / regulation of actin polymerization or depolymerization / synapse maturation / peptide alpha-N-acetyltransferase activity / acetyl-CoA binding / modification of postsynaptic actin cytoskeleton / regulation of transepithelial transport / negative regulation of actin filament bundle assembly / adenyl-nucleotide exchange factor activity / morphogenesis of a polarized epithelium / bBAF complex / npBAF complex / brahma complex / postsynaptic actin cytoskeleton organization / nBAF complex / protein localization to adherens junction / postsynaptic actin cytoskeleton / Tat protein binding / structural constituent of postsynaptic actin cytoskeleton / GBAF complex / positive regulation of actin filament bundle assembly / negative regulation of actin filament polymerization / regulation of G0 to G1 transition / dense body / Formation of annular gap junctions / Gap junction degradation / Signaling by ROBO receptors / Cell-extracellular matrix interactions / Folding of actin by CCT/TriC / regulation of actin filament polymerization / apical protein localization / regulation of double-strand break repair / regulation of nucleotide-excision repair / adherens junction assembly / Prefoldin mediated transfer of substrate to CCT/TriC / RSC-type complex / RHOF GTPase cycle / Adherens junctions interactions / N-acetyltransferase activity / tight junction / positive regulation of ATP-dependent activity / PCP/CE pathway / regulation of norepinephrine uptake / proline-rich region binding / Sensory processing of sound by outer hair cells of the cochlea / positive regulation of ruffle assembly / regulation of mitotic metaphase/anaphase transition / Interaction between L1 and Ankyrins / Sensory processing of sound by inner hair cells of the cochlea / SWI/SNF complex / positive regulation of double-strand break repair / regulation of synaptic vesicle endocytosis / positive regulation of T cell differentiation / negative regulation of stress fiber assembly / apical junction complex / establishment or maintenance of cell polarity / NuA4 histone acetyltransferase complex / regulation of cyclin-dependent protein serine/threonine kinase activity / maintenance of blood-brain barrier / cortical cytoskeleton / positive regulation of actin filament polymerization / positive regulation of stem cell population maintenance / protein acetylation / nitric-oxide synthase binding / positive regulation of epithelial cell migration / Recycling pathway of L1 / kinesin binding / regulation of G1/S transition of mitotic cell cycle / brush border / calyx of Held / negative regulation of cell differentiation / positive regulation of double-strand break repair via homologous recombination / actin monomer binding / EPH-ephrin mediated repulsion of cells / RHO GTPases Activate WASPs and WAVEs / RHO GTPases activate IQGAPs / positive regulation of myoblast differentiation / regulation of protein localization to plasma membrane / Transferases; Acyltransferases; Transferring groups other than aminoacyl groups / phosphatidylinositol-4,5-bisphosphate binding / EPHB-mediated forward signaling / substantia nigra development / phosphotyrosine residue binding / axonogenesis / negative regulation of protein binding / neural tube closure / 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 / DNA Damage Recognition in GG-NER / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.5 Å | ||||||
Authors | Rebowski, G. / Boczkowska, M. / Dominguez, R. | ||||||
Funding support | United States, 1items
| ||||||
Citation | Journal: Sci Adv / Year: 2020 Title: Mechanism of actin N-terminal acetylation. Authors: Rebowski, G. / Boczkowska, M. / Drazic, A. / Ree, R. / Goris, M. / Arnesen, T. / Dominguez, R. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 6nbw.cif.gz | 273.7 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb6nbw.ent.gz | 218 KB | Display | PDB format |
PDBx/mmJSON format | 6nbw.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6nbw_validation.pdf.gz | 1.4 MB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 6nbw_full_validation.pdf.gz | 1.4 MB | Display | |
Data in XML | 6nbw_validation.xml.gz | 28.9 KB | Display | |
Data in CIF | 6nbw_validation.cif.gz | 39.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/nb/6nbw ftp://data.pdbj.org/pub/pdb/validation_reports/nb/6nbw | HTTPS FTP |
-Related structure data
Related structure data | 6nasC 6nbeC 2pbdS S: Starting model for refinement C: citing same article (ref.) |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-Components
-Protein , 3 types, 3 molecules ANP
#1: Protein | Mass: 41664.484 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P60709 |
---|---|
#2: Protein | Mass: 25923.076 Da / Num. of mol.: 1 / Fragment: residues 56-286 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: NAA80, FUS2, NAT6 / Production host: Escherichia coli (E. coli) References: UniProt: Q93015, Transferases; Acyltransferases; Transferring groups other than aminoacyl groups |
#3: Protein | Mass: 15071.222 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PFN1 / Production host: Escherichia coli (E. coli) / References: UniProt: P07737 |
-Non-polymers , 7 types, 211 molecules
#4: Chemical | ChemComp-CA / | ||||||
---|---|---|---|---|---|---|---|
#5: Chemical | ChemComp-ATP / | ||||||
#6: Chemical | ChemComp-LAB / | ||||||
#7: Chemical | #8: Chemical | ChemComp-SOP / [( | #9: Chemical | ChemComp-MES / | #10: Water | ChemComp-HOH / | |
-Details
Has ligand of interest | N |
---|
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 2.65 Å3/Da / Density % sol: 53.56 % |
---|---|
Crystal grow | Temperature: 290 K / Method: vapor diffusion, hanging drop / pH: 6.5 / Details: 15% PEG 3350, 50mM MES pH6.2, 50mM NH4NO3 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: CHESS / Beamline: F1 / Wavelength: 0.9775 Å |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Nov 27, 2017 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9775 Å / Relative weight: 1 |
Reflection | Resolution: 2.496→50 Å / Num. obs: 28132 / % possible obs: 100 % / Redundancy: 13.1 % / Biso Wilson estimate: 33 Å2 / Rmerge(I) obs: 0.116 / Net I/σ(I): 21 |
Reflection shell | Resolution: 2.5→2.59 Å / Redundancy: 13.3 % / Rmerge(I) obs: 0.563 / Mean I/σ(I) obs: 4 / Num. unique obs: 2785 / % possible all: 100 |
-Processing
Software |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 2PBD Resolution: 2.5→26.1 Å / SU ML: 0.26 / Cross valid method: THROUGHOUT / σ(F): 1.36 / Phase error: 20.17 / Stereochemistry target values: ML
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 138.16 Å2 / Biso mean: 43.413 Å2 / Biso min: 24.15 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 2.5→26.1 Å
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 10
|