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- PDB-5yc2: Crystal structure of inner membrane protein Bqt4 in complex with ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5yc2 | ||||||
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Title | Crystal structure of inner membrane protein Bqt4 in complex with telomeric protein Rap1 | ||||||
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![]() | MEMBRANE PROTEIN / Choromosome organization / Teleomere bouquet / Nuclear envelope / Spore formation | ||||||
Function / homology | ![]() meiotic telomere tethering at nuclear periphery / telomere-nuclear envelope anchor activity / nuclear membrane complex Bqt3-Bqt4 / meiotic attachment of telomeric heterochromatin to spindle pole body / meiotic spindle pole body / nucleus leading edge / mitotic telomere tethering at nuclear periphery / Removal of the Flap Intermediate from the C-strand / meiotic attachment of telomere to nuclear envelope / chromosome, telomeric repeat region ...meiotic telomere tethering at nuclear periphery / telomere-nuclear envelope anchor activity / nuclear membrane complex Bqt3-Bqt4 / meiotic attachment of telomeric heterochromatin to spindle pole body / meiotic spindle pole body / nucleus leading edge / mitotic telomere tethering at nuclear periphery / Removal of the Flap Intermediate from the C-strand / meiotic attachment of telomere to nuclear envelope / chromosome, telomeric repeat region / protection from non-homologous end joining at telomere / SUMO is conjugated to E1 (UBA2:SAE1) / SUMOylation of nuclear envelope proteins / SUMO is transferred from E1 to E2 (UBE2I, UBC9) / SUMO is proteolytically processed / SUMOylation of transcription factors / meiotic telomere clustering / Postmitotic nuclear pore complex (NPC) reformation / SUMOylation of transcription cofactors / telomere maintenance via telomere lengthening / SUMOylation of DNA damage response and repair proteins / shelterin complex / SUMOylation of DNA replication proteins / septin ring / SUMOylation of SUMOylation proteins / nuclear telomere cap complex / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / SUMOylation of RNA binding proteins / telomere capping / SUMOylation of chromatin organization proteins / nuclear inner membrane / telomeric DNA binding / ubiquitin-like protein ligase binding / protein sumoylation / telomere organization / telomere maintenance / condensed nuclear chromosome / PML body / protein tag activity / nuclear envelope / cell division / regulation of DNA-templated transcription / DNA binding / identical protein binding / membrane / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Chen, Y. / Hu, C. | ||||||
![]() | ![]() Title: Structural insights into chromosome attachment to the nuclear envelope by an inner nuclear membrane protein Bqt4 in fission yeast. Authors: Hu, C. / Inoue, H. / Sun, W. / Takeshita, Y. / Huang, Y. / Xu, Y. / Kanoh, J. / Chen, Y. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 184.5 KB | Display | ![]() |
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PDB format | ![]() | 148.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 450.6 KB | Display | ![]() |
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Full document | ![]() | 453.4 KB | Display | |
Data in XML | ![]() | 16.7 KB | Display | |
Data in CIF | ![]() | 22 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5ycaC ![]() 6a6wC ![]() 5ybxS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Assembly
Deposited unit | ![]()
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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 23570.859 Da / Num. of mol.: 2 / Mutation: Q61E Source method: isolated from a genetically manipulated source Details: SUMO (residue 20 to 92) tagged Bqt4 (residue 8 to 140) Source: (gene. exp.) ![]() ![]() ![]() ![]() Strain: ATCC 204508 / S288c, 972 / ATCC 24843 / Gene: SMT3, YDR510W, D9719.15, bqt4, SPBC19C7.10 / Production host: ![]() ![]() #2: Protein/peptide | Mass: 2003.059 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: Bqt4 binding motif of telomeric protein Rap1 Source: (gene. exp.) ![]() ![]() Strain: 972 / ATCC 24843 / Gene: rap1, SPBC1778.02 / Production host: ![]() ![]() #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.5 Å3/Da / Density % sol: 50.71 % / Description: Snowflake |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: 0.1M HEPES sodium pH 7.5, 10% v/v 2-Propanol, 20% w/v Polyethyleneglycol 4000. Temp details: crystal culture in cold room |
-Data collection
Diffraction | Mean temperature: 100 K / Ambient temp details: Liquid nitrogen |
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Diffraction source | Source: ![]() ![]() |
Detector | Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Dec 27, 2015 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97853 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→39.056 Å / Num. obs: 12761 / % possible obs: 98 % / Redundancy: 1 % / Biso Wilson estimate: 46.84 Å2 / Net I/σ(I): 1.7 |
Reflection shell | Resolution: 2.7→2.8 Å / Redundancy: 2.9 % / Rmerge(I) obs: 0.324 / Mean I/σ(I) obs: 2.428 / CC1/2: 0.894 / Rpim(I) all: 0.216 / Rrim(I) all: 0.391 / Χ2: 0.501 / % possible all: 94.8 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 5YBX Resolution: 2.704→39.056 Å / SU ML: 0.38 / Cross valid method: FREE R-VALUE / σ(F): 2.01 / Phase error: 28.09
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 134.01 Å2 / Biso mean: 53.5988 Å2 / Biso min: 26.7 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 2.704→39.056 Å
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Refine LS restraints |
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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