+
Open data
-
Basic information
Entry | Database: PDB / ID: 1n0w | ||||||
---|---|---|---|---|---|---|---|
Title | Crystal structure of a RAD51-BRCA2 BRC repeat complex | ||||||
![]() |
| ||||||
![]() | GENE REGULATION/ANTITUMOR PROTEIN / DNA repair / homologous recombination / breast cancer susceptibility / RecA-like ATPase / protein complex / GENE REGULATION-ANTITUMOR PROTEIN COMPLEX | ||||||
Function / homology | ![]() BRCA2-MAGE-D1 complex / negative regulation of mammary gland epithelial cell proliferation / presynaptic intermediate filament cytoskeleton / mitotic recombination-dependent replication fork processing / cellular response to camptothecin / chromosome organization involved in meiotic cell cycle / establishment of protein localization to telomere / telomere maintenance via telomere lengthening / positive regulation of DNA ligation / Impaired BRCA2 translocation to the nucleus ...BRCA2-MAGE-D1 complex / negative regulation of mammary gland epithelial cell proliferation / presynaptic intermediate filament cytoskeleton / mitotic recombination-dependent replication fork processing / cellular response to camptothecin / chromosome organization involved in meiotic cell cycle / establishment of protein localization to telomere / telomere maintenance via telomere lengthening / positive regulation of DNA ligation / Impaired BRCA2 translocation to the nucleus / Impaired BRCA2 binding to SEM1 (DSS1) / double-strand break repair involved in meiotic recombination / nuclear ubiquitin ligase complex / cellular response to hydroxyurea / replication-born double-strand break repair via sister chromatid exchange / lateral element / telomere maintenance via recombination / DNA recombinase assembly / histone H4 acetyltransferase activity / histone H3 acetyltransferase activity / regulation of DNA damage checkpoint / mitotic recombination / Impaired BRCA2 binding to PALB2 / DNA strand invasion / HDR through MMEJ (alt-NHEJ) / gamma-tubulin binding / DNA strand exchange activity / reciprocal meiotic recombination / DNA repair complex / Defective homologous recombination repair (HRR) due to BRCA1 loss of function / Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA1 binding function / Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA2/RAD51/RAD51C binding function / Homologous DNA Pairing and Strand Exchange / Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA) / response to UV-C / oocyte maturation / Resolution of D-loop Structures through Holliday Junction Intermediates / single-stranded DNA helicase activity / inner cell mass cell proliferation / ATP-dependent DNA damage sensor activity / DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator / hematopoietic stem cell proliferation / HDR through Single Strand Annealing (SSA) / Impaired BRCA2 binding to RAD51 / regulation of double-strand break repair via homologous recombination / nuclear chromosome / female gonad development / replication fork processing / male meiosis I / DNA unwinding involved in DNA replication / Transcriptional Regulation by E2F6 / Presynaptic phase of homologous DNA pairing and strand exchange / centrosome duplication / response to X-ray / intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / ATP-dependent activity, acting on DNA / interstrand cross-link repair / DNA polymerase binding / condensed chromosome / positive regulation of mitotic cell cycle / meiotic cell cycle / regulation of cytokinesis / condensed nuclear chromosome / secretory granule / male germ cell nucleus / cellular response to ionizing radiation / nucleotide-excision repair / response to gamma radiation / regulation of protein phosphorylation / double-strand break repair via homologous recombination / HDR through Homologous Recombination (HRR) / brain development / PML body / Meiotic recombination / cellular senescence / double-strand break repair / site of double-strand break / single-stranded DNA binding / spermatogenesis / double-stranded DNA binding / DNA recombination / protease binding / chromosome, telomeric region / mitochondrial matrix / DNA repair / centrosome / DNA damage response / chromatin binding / regulation of DNA-templated transcription / chromatin / nucleolus / positive regulation of DNA-templated transcription / perinuclear region of cytoplasm / enzyme binding / ATP hydrolysis activity / protein-containing complex / mitochondrion / nucleoplasm / ATP binding / identical protein binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Pellegrini, L. / Yu, D.S. / Lo, T. / Anand, S. / Lee, M. / Blundell, T.L. / Venkitaraman, A.R. | ||||||
![]() | ![]() Title: Insights into DNA recombination from the structure of a RAD51-BRCA2 complex Authors: Pellegrini, L. / Yu, D.S. / Lo, T. / Anand, S. / Lee, M. / Blundell, T.L. / Venkitaraman, A.R. | ||||||
History |
| ||||||
Remark 999 | SEQUENCE All chains in the entry are part of an engineered, chimeric protein construct. In the ...SEQUENCE All chains in the entry are part of an engineered, chimeric protein construct. In the construct, the amino-to-carboxyl order of the chains is: C-B-L-A. Chain C is a GSMG sequence that comes from the expression vector, B is the BRCA2 BRC repeat, L is the TGSTGSTGSTGSMG sequence linking chains B and A, and chain A is the RAD51 ATpase domain. Chain C appears as a separate entity because the two initial residues of chain B, 1517-8, are not visible in the density map. Likewise, the linker is not visible in the density map, with the exception of the first three residues:TGS. |
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 67.5 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 52.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 467.6 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 469 KB | Display | |
Data in XML | ![]() | 14.6 KB | Display | |
Data in CIF | ![]() | 20.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||
Unit cell |
| ||||||||
Details | The asymmetric unit contains one biological unit, constituted by one chain A, one chain B and one chain C |
-
Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 26855.346 Da / Num. of mol.: 1 / Fragment: ATPase domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
---|
-Protein/peptide , 3 types, 3 molecules BLC
#2: Protein/peptide | Mass: 3966.598 Da / Num. of mol.: 1 / Fragment: BRC repeat type 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
---|---|
#3: Protein/peptide | Mass: 1234.091 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: this peptide links the BRCA2 to the RAD51 / Plasmid: pGAT3 / Species (production host): Escherichia coli / Production host: ![]() ![]() |
#4: Protein/peptide | Mass: 397.287 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: this peptide comes from the expression vector and is linked to the N-terminus of BRCA2 Plasmid: pGAT3 / Species (production host): Escherichia coli / Production host: ![]() ![]() |
-Non-polymers , 4 types, 254 molecules ![](data/chem/img/MG.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/EDO.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/EDO.gif)
![](data/chem/img/HOH.gif)
#5: Chemical | ChemComp-MG / | ||
---|---|---|---|
#6: Chemical | ChemComp-CL / | ||
#7: Chemical | ChemComp-EDO / #8: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.01 Å3/Da / Density % sol: 38.95 % / Description: Freidel pairs were used. |
---|---|
Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 7.2 Details: ETHYLENE GLYCOL, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
Crystal grow | *PLUS Temperature: 18 ℃ |
Components of the solutions | *PLUS Conc.: 25 % / Common name: ethylene glycol |
-Data collection
Diffraction | Mean temperature: 100 K | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Diffraction source | Source: ![]() ![]() ![]() | |||||||||
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Apr 7, 2002 | |||||||||
Radiation | Monochromator: channel - cut Si monochromator + cylindrical grazing incidence mirror Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||
Radiation wavelength |
| |||||||||
Reflection | Resolution: 1.7→24.85 Å / Num. obs: 55746 / % possible obs: 99.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 7 % / Biso Wilson estimate: 16.9 Å2 / Rmerge(I) obs: 0.077 / Rsym value: 0.077 / Net I/σ(I): 23.5 | |||||||||
Reflection shell | Resolution: 1.7→1.73 Å / Rmerge(I) obs: 0.321 / Mean I/σ(I) obs: 6.5 / Rsym value: 0.321 / % possible all: 99.9 | |||||||||
Reflection | *PLUS Highest resolution: 1.7 Å / Num. obs: 29143 / Num. measured all: 204230 | |||||||||
Reflection shell | *PLUS % possible obs: 99.9 % |
-
Processing
Software |
| ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Details: The structure was refined against the peak Se K edge wavelength dataset. Selenomethionine residues (residue name MSE) were used in the refinement, and are present in the deposited coordinate ...Details: The structure was refined against the peak Se K edge wavelength dataset. Selenomethionine residues (residue name MSE) were used in the refinement, and are present in the deposited coordinate file. Freidel pairs were used.
| ||||||||||||||||||||
Displacement parameters | Biso mean: 21.1 Å2 | ||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.7→24.85 Å
| ||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.7 Å / Lowest resolution: 24.8 Å | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS Type: c_angle_deg / Dev ideal: 1.229 |