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- PDB-4cht: Crystal structure of the human topoisomerase III alpha-RMI1 compl... -

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Basic information

Entry
Database: PDB / ID: 4cht
TitleCrystal structure of the human topoisomerase III alpha-RMI1 complex with bound calcium ion
Components
  • DNA TOPOISOMERASE 3-ALPHA
  • RECQ-MEDIATED GENOME INSTABILITY PROTEIN 1
KeywordsCELL CYCLE / DOUBLE HOLLIDAY JUNCTION DISSOLUTION / DECATENATION / MINIMAL DISSOLVASOME
Function / homology
Function and homology information


reduction of food intake in response to dietary excess / RecQ family helicase-topoisomerase III complex / DNA topoisomerase activity / resolution of DNA recombination intermediates / chromosome separation / DNA topoisomerase / DNA topoisomerase type I (single strand cut, ATP-independent) activity / resolution of meiotic recombination intermediates / mitochondrial DNA metabolic process / Impaired BRCA2 binding to PALB2 ...reduction of food intake in response to dietary excess / RecQ family helicase-topoisomerase III complex / DNA topoisomerase activity / resolution of DNA recombination intermediates / chromosome separation / DNA topoisomerase / DNA topoisomerase type I (single strand cut, ATP-independent) activity / resolution of meiotic recombination intermediates / mitochondrial DNA metabolic process / Impaired BRCA2 binding to PALB2 / 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) / Resolution of D-loop Structures through Holliday Junction Intermediates / HDR through Single Strand Annealing (SSA) / Impaired BRCA2 binding to RAD51 / DNA topological change / Presynaptic phase of homologous DNA pairing and strand exchange / response to glucose / meiotic cell cycle / double-strand break repair via homologous recombination / HDR through Homologous Recombination (HRR) / G2/M DNA damage checkpoint / multicellular organism growth / PML body / Meiotic recombination / glucose homeostasis / single-stranded DNA binding / Processing of DNA double-strand break ends / Regulation of TP53 Activity through Phosphorylation / DNA replication / nuclear body / mitochondrial matrix / nucleotide binding / DNA binding / zinc ion binding / nucleoplasm / nucleus
Similarity search - Function
RecQ-mediated genome instability protein 1, N-terminal domain / RecQ-mediated genome instability protein Rmi1, C-terminal domain / RecQ-mediated genome instability protein 1, C-terminal OB-fold domain / RecQ-mediated genome instability protein 1, N-terminal helical domain superfamily / : / Recq-mediated genome instability protein 1, C-terminal OB-fold / RMI1, N-terminal helical domain / DUF1767 / Zinc finger GRF-type profile. / DNA topoisomerase 3-like, TOPRIM domain ...RecQ-mediated genome instability protein 1, N-terminal domain / RecQ-mediated genome instability protein Rmi1, C-terminal domain / RecQ-mediated genome instability protein 1, C-terminal OB-fold domain / RecQ-mediated genome instability protein 1, N-terminal helical domain superfamily / : / Recq-mediated genome instability protein 1, C-terminal OB-fold / RMI1, N-terminal helical domain / DUF1767 / Zinc finger GRF-type profile. / DNA topoisomerase 3-like, TOPRIM domain / Zinc finger, GRF-type / GRF zinc finger / RecQ mediated genome instability protein 1, N-terminal / RecQ mediated genome instability protein, N-terminal OB-fold superfamily / RMI1, N-terminal OB-fold domain / DNA topoisomerase, type IA, zn finger / Topoisomerase DNA binding C4 zinc finger / Topoisomerase I, domain 3 / Topoisomerase I; domain 2 / Topoisomerase I, domain 2 / Rossmann fold - #140 / Topoisomerase I; domain 4 / Topoisomerase I, domain 4 / DNA topoisomerase, type IA / DNA topoisomerase, type IA, central region, subdomain 2 / DNA topoisomerase, type IA, active site / Topoisomerase (Topo) IA-type active site signature. / Topoisomerase (Topo) IA-type catalytic domain profile. / DNA topoisomerase, type IA, domain 2 / DNA topoisomerase, type IA, DNA-binding domain / DNA topoisomerase, type IA, central / DNA topoisomerase, type IA, central region, subdomain 1 / DNA topoisomerase, type IA, central region, subdomain 3 / DNA topoisomerase, type IA, core domain / DNA topoisomerase / Bacterial DNA topoisomeraes I ATP-binding domain / Bacterial DNA topoisomerase I DNA-binding domain / Topoisomerase I; domain 3 / TOPRIM / Toprim domain / Toprim domain profile. / TOPRIM domain / Helicase, Ruva Protein; domain 3 / Distorted Sandwich / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / Beta Barrel / Rossmann fold / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
DNA topoisomerase 3-alpha / RecQ-mediated genome instability protein 1
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.25 Å
AuthorsBocquet, N. / Bunker, R.D. / Thoma, N.H.
CitationJournal: Nat.Struct.Mol.Biol. / Year: 2014
Title: Structural and Mechanistic Insight Into Holliday-Junction Dissolution by Topoisomerase Iiialpha and Rmi1
Authors: Bocquet, N. / Bizard, A.H. / Abdulrahman, W. / Larsen, N.B. / Faty, M. / Cavadini, S. / Bunker, R.D. / Kowalczykowski, S.C. / Cejka, P. / Hickson, I.D. / Thoma, N.H.
History
DepositionDec 4, 2013Deposition site: PDBE / Processing site: PDBE
Revision 1.0Feb 12, 2014Provider: repository / Type: Initial release
Revision 1.1Feb 19, 2014Group: Database references
Revision 1.2Mar 19, 2014Group: Database references
Revision 1.3Apr 3, 2019Group: Data collection / Other / Source and taxonomy
Category: entity_src_gen / pdbx_database_proc / pdbx_database_status
Item: _entity_src_gen.pdbx_host_org_cell_line / _pdbx_database_status.recvd_author_approval
Revision 1.4Dec 20, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: DNA TOPOISOMERASE 3-ALPHA
B: RECQ-MEDIATED GENOME INSTABILITY PROTEIN 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)111,3263
Polymers111,2862
Non-polymers401
Water905
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3150 Å2
ΔGint-20.2 kcal/mol
Surface area38410 Å2
MethodPISA
Unit cell
Length a, b, c (Å)93.360, 93.360, 381.620
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number92
Space group name H-MP41212

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Components

#1: Protein DNA TOPOISOMERASE 3-ALPHA / DNA TOPOISOMERASE III ALPHA


Mass: 86641.688 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Cell line (production host): High Five / Production host: TRICHOPLUSIA NI (cabbage looper) / References: UniProt: Q13472, DNA topoisomerase
#2: Protein RECQ-MEDIATED GENOME INSTABILITY PROTEIN 1 / BLM-ASSOCIATED PROTEIN OF 75 KDA / BLAP75 / FAAP75


Mass: 24644.457 Da / Num. of mol.: 1 / Fragment: RESIDUES 1-219
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Cell line (production host): High Five / Production host: TRICHOPLUSIA NI (cabbage looper) / References: UniProt: Q9H9A7
#3: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Ca
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 5.4 Å3/Da / Density % sol: 77 % / Description: NONE
Crystal growpH: 7
Details: 8% (W/V) PEG 5000 MME, 200 MM CALCIUM CITRATE, 100 MM TRIS/HCL PH 7.0

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 1
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Sep 19, 2010 / Details: MIRRORS
RadiationMonochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.25→65.05 Å / Num. obs: 27765 / % possible obs: 99.8 % / Observed criterion σ(I): -3 / Redundancy: 5.3 % / Biso Wilson estimate: 89.41 Å2 / Rmerge(I) obs: 0.16 / Net I/σ(I): 8.2
Reflection shellResolution: 3.25→3.45 Å / Redundancy: 5.3 % / Rmerge(I) obs: 0.78 / Mean I/σ(I) obs: 2 / % possible all: 99.9

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Processing

Software
NameVersionClassification
BUSTER2.11.4refinement
XDSdata reduction
XDSAIMLESSdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 4CGY

4cgy


Resolution: 3.25→65.05 Å / Cor.coef. Fo:Fc: 0.9089 / Cor.coef. Fo:Fc free: 0.8827 / SU R Cruickshank DPI: 1.559 / Cross valid method: THROUGHOUT / σ(F): 0 / SU R Blow DPI: 2.132 / SU Rfree Blow DPI: 0.354 / SU Rfree Cruickshank DPI: 0.357
RfactorNum. reflection% reflectionSelection details
Rfree0.2245 1387 5.01 %RANDOM
Rwork0.1968 ---
obs0.1981 27665 99.69 %-
Displacement parametersBiso mean: 80.98 Å2
Baniso -1Baniso -2Baniso -3
1--11.6037 Å20 Å20 Å2
2---11.6037 Å20 Å2
3---23.2075 Å2
Refine analyzeLuzzati coordinate error obs: 0.686 Å
Refinement stepCycle: LAST / Resolution: 3.25→65.05 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6632 0 1 5 6638
Refine LS restraints
Refine-IDTypeDev idealNumberRestraint functionWeight
X-RAY DIFFRACTIONt_bond_d0.016780HARMONIC2
X-RAY DIFFRACTIONt_angle_deg1.069201HARMONIC2
X-RAY DIFFRACTIONt_dihedral_angle_d3174SINUSOIDAL2
X-RAY DIFFRACTIONt_incorr_chiral_ct
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_trig_c_planes185HARMONIC2
X-RAY DIFFRACTIONt_gen_planes968HARMONIC5
X-RAY DIFFRACTIONt_it6780HARMONIC20
X-RAY DIFFRACTIONt_nbd
X-RAY DIFFRACTIONt_omega_torsion2.7
X-RAY DIFFRACTIONt_other_torsion3.06
X-RAY DIFFRACTIONt_improper_torsion
X-RAY DIFFRACTIONt_chiral_improper_torsion880SEMIHARMONIC5
X-RAY DIFFRACTIONt_sum_occupancies
X-RAY DIFFRACTIONt_utility_distance
X-RAY DIFFRACTIONt_utility_angle
X-RAY DIFFRACTIONt_utility_torsion
X-RAY DIFFRACTIONt_ideal_dist_contact7358SEMIHARMONIC4
LS refinement shellResolution: 3.25→3.37 Å / Total num. of bins used: 14
RfactorNum. reflection% reflection
Rfree0.2784 148 5.19 %
Rwork0.2511 2704 -
all0.2525 2852 -
obs--99.69 %
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
10.3742-0.1078-0.03541.31610.3821.602-0.03290.019-0.0488-0.1020.01410.1493-0.11970.18450.01880.0176-0.1140.0294-0.08940.0032-0.0718-20.8577.531831.4422
22.24472.49642.19152.83622.67122.9437-0.1807-0.09320.1736-0.0888-0.09710.0743-0.2908-0.16660.27780.0405-0.0398-0.11290.0959-0.0202-0.0722-50.042-13.2211-9.5263
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1CHAIN A
2X-RAY DIFFRACTION2CHAIN B

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