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- PDB-1jm7: Solution structure of the BRCA1/BARD1 RING-domain heterodimer -

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Basic information

Entry
Database: PDB / ID: 1jm7
TitleSolution structure of the BRCA1/BARD1 RING-domain heterodimer
Components
  • BRCA1-ASSOCIATED RING DOMAIN PROTEIN 1
  • BREAST CANCER TYPE 1 SUSCEPTIBILITY PROTEIN
KeywordsANTITUMOR / BRCA1 / BARD1 / RING finger / zinc-binding protein / heterodimer / ubiquitin ligase
Function / homology
Function and homology information


negative regulation of mRNA 3'-end processing / histone H2AK127 ubiquitin ligase activity / histone H2AK129 ubiquitin ligase activity / Defective DNA double strand break response due to BRCA1 loss of function / Defective DNA double strand break response due to BARD1 loss of function / BRCA1-BARD1 complex / BRCA1-B complex / BRCA1-A complex / BRCA1-C complex / negative regulation of centriole replication ...negative regulation of mRNA 3'-end processing / histone H2AK127 ubiquitin ligase activity / histone H2AK129 ubiquitin ligase activity / Defective DNA double strand break response due to BRCA1 loss of function / Defective DNA double strand break response due to BARD1 loss of function / BRCA1-BARD1 complex / BRCA1-B complex / BRCA1-A complex / BRCA1-C complex / negative regulation of centriole replication / random inactivation of X chromosome / ubiquitin-modified histone reader activity / gamma-tubulin ring complex / negative regulation of intracellular estrogen receptor signaling pathway / chordate embryonic development / cellular response to indole-3-methanol / regulation of phosphorylation / DNA strand resection involved in replication fork processing / nuclear ubiquitin ligase complex / homologous recombination / negative regulation of fatty acid biosynthetic process / tissue homeostasis / Regulation of MITF-M-dependent genes involved in DNA replication, damage repair and senescence / lateral element / mitotic G2/M transition checkpoint / negative regulation of protein export from nucleus / regulation of DNA damage checkpoint / Impaired BRCA2 binding to PALB2 / XY body / DNA repair complex / RNA polymerase binding / DNA damage tolerance / protein K6-linked ubiquitination / centrosome cycle / HDR through Single Strand Annealing (SSA) / response to ionizing radiation / Homologous DNA Pairing and Strand Exchange / 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 / Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA) / negative regulation of gene expression via chromosomal CpG island methylation / Resolution of D-loop Structures through Holliday Junction Intermediates / mitotic G2 DNA damage checkpoint signaling / Transcriptional Regulation by E2F6 / Impaired BRCA2 binding to RAD51 / negative regulation of cell cycle / negative regulation of reactive oxygen species metabolic process / positive regulation of vascular endothelial growth factor production / Presynaptic phase of homologous DNA pairing and strand exchange / ubiquitin ligase complex / regulation of DNA repair / negative regulation of extrinsic apoptotic signaling pathway via death domain receptors / SUMOylation of DNA damage response and repair proteins / protein autoubiquitination / Meiotic synapsis / positive regulation of DNA repair / male germ cell nucleus / cellular response to ionizing radiation / TP53 Regulates Transcription of DNA Repair Genes / Nonhomologous End-Joining (NHEJ) / chromosome segregation / tubulin binding / negative regulation of cell growth / RING-type E3 ubiquitin transferase / G2/M DNA damage checkpoint / double-strand break repair via homologous recombination / Meiotic recombination / HDR through Homologous Recombination (HRR) / cellular response to tumor necrosis factor / intrinsic apoptotic signaling pathway in response to DNA damage / kinase binding / fatty acid biosynthetic process / Metalloprotease DUBs / positive regulation of angiogenesis / cytoplasmic ribonucleoprotein granule / p53 binding / ubiquitin-protein transferase activity / positive regulation of protein catabolic process / UCH proteinases / KEAP1-NFE2L2 pathway / double-strand break repair / chromosome / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / Neddylation / Processing of DNA double-strand break ends / Regulation of TP53 Activity through Phosphorylation / damaged DNA binding / transcription coactivator activity / regulation of cell cycle / transcription cis-regulatory region binding / nuclear speck / nuclear body / protein ubiquitination / positive regulation of apoptotic process / chromatin remodeling / ribonucleoprotein complex / protein heterodimerization activity / DNA repair / negative regulation of DNA-templated transcription
Similarity search - Function
BARD1, Zinc finger, RING-type / zf-RING of BARD1-type protein / Breast cancer type 1 susceptibility protein (BRCA1) / BRCA1, serine-rich domain / BRCA1-associated / Serine-rich domain associated with BRCT / Zinc finger, C3HC4 RING-type / Zinc finger, C3HC4 type (RING finger) / BRCA1 C Terminus (BRCT) domain / Zinc/RING finger domain, C3HC4 (zinc finger) ...BARD1, Zinc finger, RING-type / zf-RING of BARD1-type protein / Breast cancer type 1 susceptibility protein (BRCA1) / BRCA1, serine-rich domain / BRCA1-associated / Serine-rich domain associated with BRCT / Zinc finger, C3HC4 RING-type / Zinc finger, C3HC4 type (RING finger) / BRCA1 C Terminus (BRCT) domain / Zinc/RING finger domain, C3HC4 (zinc finger) / Herpes Virus-1 / breast cancer carboxy-terminal domain / BRCT domain profile. / BRCT domain / BRCT domain superfamily / Zinc finger, RING-type, conserved site / Zinc finger RING-type signature. / Ring finger / Ankyrin repeat profile. / Ankyrin repeats (3 copies) / Ankyrin repeat region circular profile. / ankyrin repeats / Ankyrin repeat / Ankyrin repeat-containing domain superfamily / Zinc finger RING-type profile. / Zinc finger, RING-type / Zinc finger, RING/FYVE/PHD-type / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Breast cancer type 1 susceptibility protein / BRCA1-associated RING domain protein 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / distance geometry simulated annealing
Model detailsBREAST CANCER TYPE 1 SUSCEPTIBILITY PROTEIN/BRCA1-ASSOCIATED RING DOMAIN PROTEIN 1 COMPLEX
AuthorsBrzovic, P.S. / Rajagopal, P. / Hoyt, D.W. / King, M.-C. / Klevit, R.E.
CitationJournal: Nat Struct Biol / Year: 2001
Title: Structure of a BRCA1-BARD1 heterodimeric RING-RING complex.
Authors: P S Brzovic / P Rajagopal / D W Hoyt / M C King / R E Klevit /
Abstract: The RING domain of the breast and ovarian cancer tumor suppressor BRCA1 interacts with multiple cognate proteins, including the RING protein BARD1. Proper function of the BRCA1 RING domain is ...The RING domain of the breast and ovarian cancer tumor suppressor BRCA1 interacts with multiple cognate proteins, including the RING protein BARD1. Proper function of the BRCA1 RING domain is critical, as evidenced by the many cancer-predisposing mutations found within this domain. We present the solution structure of the heterodimer formed between the RING domains of BRCA1 and BARD1. Comparison with the RING homodimer of the V(D)J recombination-activating protein RAG1 reveals the structural diversity of complexes formed by interactions between different RING domains. The BRCA1-BARD1 structure provides a model for its ubiquitin ligase activity, illustrates how the BRCA1 RING domain can be involved in associations with multiple protein partners and provides a framework for understanding cancer-causing mutations at the molecular level.
History
DepositionJul 17, 2001Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 3, 2001Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_conn_angle / pdbx_struct_oper_list / struct_conn / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_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_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_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.4May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: BREAST CANCER TYPE 1 SUSCEPTIBILITY PROTEIN
B: BRCA1-ASSOCIATED RING DOMAIN PROTEIN 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)26,2506
Polymers25,9882
Non-polymers2624
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)14 / 25structures with the least restraint violations, structures with the lowest energy
RepresentativeModel #2closest to the average

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Components

#1: Protein BREAST CANCER TYPE 1 SUSCEPTIBILITY PROTEIN / BRCA1


Mass: 12819.168 Da / Num. of mol.: 1 / Fragment: RING-Domain
Source method: isolated from a genetically manipulated source
Details: residues 104-112 of chain A and 123-142 of chain B are missing in each model due to disorder.
Source: (gene. exp.) Homo sapiens (human) / Gene: BRCA1 / Plasmid: PET11a / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 DE3 / References: UniProt: P38398
#2: Protein BRCA1-ASSOCIATED RING DOMAIN PROTEIN 1 / BARD1


Mass: 13169.250 Da / Num. of mol.: 1 / Fragment: RING-Domain
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: BARD1 / Plasmid: PET11a / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 DE3 / References: UniProt: Q99728
#3: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Zn

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D 15N-separated NOESY
1214D 13C-separated NOESY
2324D 13C-separated NOESY
2423D 15N/13C-separated NOESY
1513D 15N/13C-separated NOESY
NMR detailsText: The structure was determined using triple-resonance NMR spectroscopy

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Sample preparation

Details
Solution-IDContentsSolvent system
1sample 1: 0.8-1.1mM U-15N,13C BRCA1; unlabeled BARD1, 25mM sodium phosphate, 0.2M NaCl, 2mM DTT. Sample 2: 0.8-1.1mM U-15N,13C BARD1; unlabeled BRCA1, 25mM sodium phosphate, 0.2M NaCl, 2mM DTT. Sample 3: 0.8-1.1mM U-15N,13C,85%-2H BRCA1; unlabeled BARD1, 25mM sodium phosphate, 0.2M NaCl, 2mM DTT. SAMPLE 4: 0.8-1.1mM U-15N,13C,85%-2H BARD1; unlabeled BRCA,1 25mM sodium phosphate, 0.2M NaCl, 2mM DTT.90% H2O/10% D2O
20.8-1.1mM U-15N,13C BARD1; unlabeled BRCA1 25mM sodium phosphate 0.2M NaCl 2mM DTT90% H2O/10% D2O
30.8-1.1mM U-15N,13C,85%-2H BRCA1; unlabeled BARD1 25mM sodium phosphate 0.2M NaCl 2mM DTT90% H2O/10% D2O
40.8-1.1mM U-15N,13C,85%-2H BARD1; unlabeled BRCA1 25mM sodium phosphate 0.2M NaCl 2mM DTT90% H2O/10% D2O
Sample conditions
Conditions-IDIonic strengthpHPressure (kPa)Temperature (K)
10.2M NaCl 6.8ambient 315 K
20.2M NaCl 6.8ambient 315 K
30.2M NaCl 6.8ambient 315 K
40.2M NaCl 6.8ambient 315 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker DMXBrukerDMX5001
Varian INOVAVarianINOVA6002
Varian INOVAVarianINOVA8003

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Processing

NMR software
NameVersionDeveloperClassification
XwinNMR2.6collection
VNMRcollection
NMRPipeDelaglio, F.processing
NMRView5Johnson, B.data analysis
CNS1Brungerstructure solution
CNSBRUNGERrefinement
RefinementMethod: distance geometry simulated annealing / Software ordinal: 1
Details: Structures are based on a total of 1664 restraints, 480 Intraresidue restraints, 475 Sequential restraints, 215 Medium-Range restraints, 256 Long-Range restraints, 82 Intermolecular ...Details: Structures are based on a total of 1664 restraints, 480 Intraresidue restraints, 475 Sequential restraints, 215 Medium-Range restraints, 256 Long-Range restraints, 82 Intermolecular restraints, 70 Hydrogen bond restraints, 16 Zinc restraints
NMR representativeSelection criteria: closest to the average
NMR ensembleConformer selection criteria: structures with the least restraint violations, structures with the lowest energy
Conformers calculated total number: 25 / Conformers submitted total number: 14

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