+Open data
-Basic information
Entry | Database: PDB / ID: 4xa1 | ||||||
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Title | Crystal Structure of the coiled-coil surrounding Skip 1 of MYH7 | ||||||
Components | Gp7-MYH7(1173-1238)-EB1 chimera protein | ||||||
Keywords | MOTOR PROTEIN / Myosin / coiled coil / skip residue / fusion / Gp7 / EB1 / MYH7 / Cardiac | ||||||
Function / homology | Function and homology information viral scaffold / protein localization to astral microtubule / regulation of slow-twitch skeletal muscle fiber contraction / cortical microtubule cytoskeleton / regulation of the force of skeletal muscle contraction / mitotic spindle astral microtubule end / protein localization to microtubule / muscle myosin complex / microtubule plus-end / muscle filament sliding ...viral scaffold / protein localization to astral microtubule / regulation of slow-twitch skeletal muscle fiber contraction / cortical microtubule cytoskeleton / regulation of the force of skeletal muscle contraction / mitotic spindle astral microtubule end / protein localization to microtubule / muscle myosin complex / microtubule plus-end / muscle filament sliding / cell projection membrane / regulation of the force of heart contraction / transition between fast and slow fiber / myosin filament / attachment of mitotic spindle microtubules to kinetochore / microtubule plus-end binding / non-motile cilium assembly / myosin II complex / adult heart development / microtubule bundle formation / cardiac muscle hypertrophy in response to stress / protein localization to centrosome / myosin complex / microtubule organizing center / sarcomere organization / virion assembly / negative regulation of microtubule polymerization / microfilament motor activity / ventricular cardiac muscle tissue morphogenesis / myofibril / mitotic spindle pole / microtubule polymerization / establishment of mitotic spindle orientation / skeletal muscle contraction / striated muscle contraction / regulation of microtubule polymerization or depolymerization / spindle midzone / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / cytoplasmic microtubule / ATP metabolic process / stress fiber / Mitotic Prometaphase / spindle assembly / EML4 and NUDC in mitotic spindle formation / cardiac muscle contraction / Loss of Nlp from mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / Recruitment of mitotic centrosome proteins and complexes / Resolution of Sister Chromatid Cohesion / Recruitment of NuMA to mitotic centrosomes / Anchoring of the basal body to the plasma membrane / regulation of heart rate / positive regulation of microtubule polymerization / sarcomere / AURKA Activation by TPX2 / ciliary basal body / muscle contraction / RHO GTPases Activate Formins / protein localization / Z disc / Separation of Sister Chromatids / The role of GTSE1 in G2/M progression after G2 checkpoint / Regulation of PLK1 Activity at G2/M Transition / actin filament binding / cell migration / microtubule / molecular adaptor activity / calmodulin binding / cadherin binding / cell division / focal adhesion / centrosome / protein kinase binding / Golgi apparatus / DNA binding / RNA binding / ATP binding / identical protein binding / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Bacillus phage phi29 (virus) Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.2 Å | ||||||
Authors | Taylor, K.C. / Buvoli, M. / Korkmaz, E.N. / Buvoli, A. / Zheng, Y. / Heinz, N.T. / Qiang, C. / Leinwand, L.A. / Rayment, I. | ||||||
Funding support | United States, 1items
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Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2015 Title: Skip residues modulate the structural properties of the myosin rod and guide thick filament assembly. Authors: Taylor, K.C. / Buvoli, M. / Korkmaz, E.N. / Buvoli, A. / Zheng, Y. / Heinze, N.T. / Cui, Q. / Leinwand, L.A. / Rayment, I. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4xa1.cif.gz | 125.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4xa1.ent.gz | 98.6 KB | Display | PDB format |
PDBx/mmJSON format | 4xa1.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xa/4xa1 ftp://data.pdbj.org/pub/pdb/validation_reports/xa/4xa1 | HTTPS FTP |
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-Related structure data
Related structure data | 4xa3C 4xa4C 4xa6C 1n04S 1yibS C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 18446.553 Da / Num. of mol.: 4 Fragment: UNP P13848 residues 1-49,UNP Q12883 residues 1173-1238,UNP Q15691 residues 211-251 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus phage phi29 (virus), (gene. exp.) Homo sapiens (human) Plasmid: pET28 / Gene: MYH7, MYHCB, MAPRE1 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) References: UniProt: P13848, UniProt: P12883, UniProt: Q15691 #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.85 Å3/Da / Density % sol: 57 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7.6 Details: 20% (w/v) polyethylene glycol methyl ether 2000, 20 mM SrCl2, 100 mM HEPES pH 7.6, 5% pentaerythritol ethoxylate (17/8 PO/OH) 797, 0.5% 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (CHAPS) |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.9792 Å |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Dec 8, 2013 |
Radiation | Monochromator: Rosenbaum-Rock high-resolution double-crystal monochromator. LN2 cooled first crystal, sagittal focusing 2nd crystal Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9792 Å / Relative weight: 1 |
Reflection | Resolution: 3.2→50 Å / Num. obs: 13198 / % possible obs: 97 % / Redundancy: 2 % / Biso Wilson estimate: 64.9 Å2 / Rmerge(I) obs: 0.03 / Net I/av σ(I): 15.5 / Net I/σ(I): 12.6 |
Reflection shell | Resolution: 3.2→3.26 Å / Redundancy: 2.1 % / Rmerge(I) obs: 0.07 / Mean I/σ(I) obs: 7.9 / % possible all: 98.7 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1N04, 1YIB Resolution: 3.2→34.861 Å / SU ML: 0.38 / Cross valid method: FREE R-VALUE / σ(F): 1.98 / Phase error: 35.91 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 48 Å2 | ||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.2→34.861 Å
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Refine LS restraints |
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LS refinement shell |
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