- PDB-5wir: Structure of the TRF1-TERB1 interface -
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Basic information
Entry
Database: PDB / ID: 5wir
Title
Structure of the TRF1-TERB1 interface
Components
TERB1-TBM
Telomeric repeat-binding factor 1
Keywords
DNA BINDING PROTEIN / meiosis / telomere / CDK phosphorylation
Function / homology
Function and homology information
positive regulation of shelterin complex assembly / negative regulation of establishment of protein localization to telomere / negative regulation of establishment of RNA localization to telomere / negative regulation of establishment of protein-containing complex localization to telomere / meiotic attachment of telomere to nuclear envelope / negative regulation of telomere maintenance via semi-conservative replication / negative regulation of exonuclease activity / negative regulation of telomeric D-loop disassembly / meiotic telomere clustering / t-circle formation ...positive regulation of shelterin complex assembly / negative regulation of establishment of protein localization to telomere / negative regulation of establishment of RNA localization to telomere / negative regulation of establishment of protein-containing complex localization to telomere / meiotic attachment of telomere to nuclear envelope / negative regulation of telomere maintenance via semi-conservative replication / negative regulation of exonuclease activity / negative regulation of telomeric D-loop disassembly / meiotic telomere clustering / t-circle formation / telomeric D-loop disassembly / shelterin complex / Telomere C-strand synthesis initiation / double-strand break repair involved in meiotic recombination / homologous chromosome pairing at meiosis / double-stranded telomeric DNA binding / Telomere C-strand (Lagging Strand) Synthesis / : / positive regulation of telomere maintenance / nuclear telomere cap complex / ankyrin repeat binding / Processive synthesis on the C-strand of the telomere / Polymerase switching on the C-strand of the telomere / Removal of the Flap Intermediate from the C-strand / G-rich strand telomeric DNA binding / telomere capping / nuclear inner membrane / DNA binding, bending / negative regulation of telomere maintenance via telomere lengthening / telomeric DNA binding / negative regulation of DNA replication / negative regulation of telomere maintenance via telomerase / Telomere Extension By Telomerase / telomere maintenance via telomerase / Packaging Of Telomere Ends / Recognition and association of DNA glycosylase with site containing an affected purine / Cleavage of the damaged purine / Recognition and association of DNA glycosylase with site containing an affected pyrimidine / Cleavage of the damaged pyrimidine / Inhibition of DNA recombination at telomere / Meiotic synapsis / telomere maintenance / DNA Damage/Telomere Stress Induced Senescence / fibrillar center / spindle / microtubule binding / chromosome, telomeric region / nuclear body / cell division / nucleolus / protein homodimerization activity / DNA binding / nucleoplasm / identical protein binding / nucleus / cytoplasm Similarity search - Function
Evidence: gel filtration, immunoprecipitation, not from IP, but we have evidence for the TERFH-TERB1 complex from GST pull down
Type
Name
Symmetry operation
Number
identity operation
1_555
x,y,z
1
Buried area
5150 Å2
ΔGint
-34 kcal/mol
Surface area
20560 Å2
Method
PISA
Unit cell
Length a, b, c (Å)
161.720, 161.720, 45.170
Angle α, β, γ (deg.)
90.00, 90.00, 120.00
Int Tables number
172
Space group name H-M
P64
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Components
#1: Protein/peptide
TERB1-TBM
Mass: 1858.284 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: The N-terminal serine remains after cleavage of the purification tag. Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: Q8NA31*PLUS
#2: Protein
Telomericrepeat-bindingfactor1 / NIMA-interacting protein 2 / TTAGGG repeat-binding factor 1 / Telomeric protein Pin2/TRF1
Mass: 23413.836 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: The N-terminal serine remains after cleavage of the purification tag. Source: (gene. exp.) Homo sapiens (human) / Gene: TERF1, PIN2, TRBF1, TRF, TRF1 / Production host: Escherichia coli (E. coli) / References: UniProt: P54274
Mass: 18.015 Da / Num. of mol.: 332 / Source method: isolated from a natural source / Formula: H2O
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Experimental details
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Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
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Sample preparation
Crystal
Density Matthews: 3.37 Å3/Da / Density % sol: 63.54 %
Crystal grow
Temperature: 289 K / Method: vapor diffusion, sitting drop / pH: 8.5 Details: TRF1-TRFH and TERB1-TBM were mixed in a 1:5 molar ratio and crystal screens set up using 0.3 microliter protein solution and 0.3 microliter reservoir solution in a sitting drop format. ...Details: TRF1-TRFH and TERB1-TBM were mixed in a 1:5 molar ratio and crystal screens set up using 0.3 microliter protein solution and 0.3 microliter reservoir solution in a sitting drop format. Diffracting crystals were obtained in 0.1 M Tris-Cl (pH 8.5) and 30% PEG 300. Crystals were cryoprotected in the crystallization solution plus 10% PEG 400 and harvested in liquid nitrogen.
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