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Open data
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Basic information
Entry | Database: PDB / ID: 4xa1 | ||||||
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Title | Crystal Structure of the coiled-coil surrounding Skip 1 of MYH7 | ||||||
![]() | Gp7-MYH7(1173-1238)-EB1 chimera protein | ||||||
![]() | MOTOR PROTEIN / Myosin / coiled coil / skip residue / fusion / Gp7 / EB1 / MYH7 / Cardiac | ||||||
Function / homology | ![]() 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 / muscle filament sliding / microtubule plus-end ...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 / muscle filament sliding / microtubule plus-end / cell projection membrane / transition between fast and slow fiber / regulation of the force of heart contraction / myosin filament / attachment of mitotic spindle microtubules to kinetochore / non-motile cilium assembly / adult heart development / microtubule bundle formation / microtubule plus-end binding / cardiac muscle hypertrophy in response to stress / myosin complex / protein localization to centrosome / ventricular cardiac muscle tissue morphogenesis / microtubule organizing center / negative regulation of microtubule polymerization / myosin II complex / microfilament motor activity / myofibril / sarcomere organization / virion assembly / mitotic spindle pole / microtubule polymerization / cytoplasmic microtubule / establishment of mitotic spindle orientation / skeletal muscle contraction / regulation of microtubule polymerization or depolymerization / spindle assembly / spindle midzone / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / striated muscle contraction / cardiac muscle contraction / stress fiber / ATP metabolic process / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Loss of Nlp from mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / Recruitment of mitotic centrosome proteins and complexes / positive regulation of microtubule polymerization / Recruitment of NuMA to mitotic centrosomes / Resolution of Sister Chromatid Cohesion / Anchoring of the basal body to the plasma membrane / regulation of heart rate / 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 / calmodulin binding / cadherin binding / cell division / focal adhesion / centrosome / protein kinase binding / Golgi apparatus / DNA binding / RNA binding / ATP binding / identical protein binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Taylor, K.C. / Buvoli, M. / Korkmaz, E.N. / Buvoli, A. / Zheng, Y. / Heinz, N.T. / Qiang, C. / Leinwand, L.A. / Rayment, I. | ||||||
Funding support | ![]()
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![]() | ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 125.4 KB | Display | ![]() |
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PDB format | ![]() | 98.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 449.7 KB | Display | ![]() |
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Full document | ![]() | 460.8 KB | Display | |
Data in XML | ![]() | 22.3 KB | Display | |
Data in CIF | ![]() | 30.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4xa3C ![]() 4xa4C ![]() 4xa6C ![]() 1n04S ![]() 1yibS C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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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.) ![]() ![]() ![]() Plasmid: pET28 / Gene: MYH7, MYHCB, MAPRE1 / Production host: ![]() ![]() References: UniProt: P13848, UniProt: P12883, UniProt: Q15691 #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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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: ![]() ![]() ![]() |
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 |
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Processing
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Refinement | Method to determine structure: ![]() 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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