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Open data
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Basic information
Entry | Database: SASBDB / ID: SASDC29 |
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![]() | Human Rev7 dimer in complex with Rev3 peptide @ 10.6 mg/mL
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Function / homology | ![]() somatic diversification of immunoglobulins involved in immune response / DNA damage response, signal transduction resulting in transcription / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function |
Biological species | ![]() ![]() |
![]() | ![]() Title: Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex. Authors: Alessandro A Rizzo / Faye-Marie Vassel / Nimrat Chatterjee / Sanjay D'Souza / Yunfeng Li / Bing Hao / Michael T Hemann / Graham C Walker / Dmitry M Korzhnev / ![]() Abstract: The translesion synthesis (TLS) polymerases Polζ and Rev1 form a complex that enables replication of damaged DNA. The Rev7 subunit of Polζ, which is a multifaceted HORMA (Hop1, Rev7, Mad2) protein ...The translesion synthesis (TLS) polymerases Polζ and Rev1 form a complex that enables replication of damaged DNA. The Rev7 subunit of Polζ, which is a multifaceted HORMA (Hop1, Rev7, Mad2) protein with roles in TLS, DNA repair, and cell-cycle control, facilitates assembly of this complex by binding Rev1 and the catalytic subunit of Polζ, Rev3. Rev7 interacts with Rev3 by a mechanism conserved among HORMA proteins, whereby an open-to-closed transition locks the ligand underneath the "safety belt" loop. Dimerization of HORMA proteins promotes binding and release of this ligand, as exemplified by the Rev7 homolog, Mad2. Here, we investigate the dimerization of Rev7 when bound to the two Rev7-binding motifs (RBMs) in Rev3 by combining in vitro analyses of Rev7 structure and interactions with a functional assay in a Rev7 cell line. We demonstrate that Rev7 uses the conventional HORMA dimerization interface both to form a homodimer when tethered by the two RBMs in Rev3 and to heterodimerize with other HORMA domains, Mad2 and p31 Structurally, the Rev7 dimer can bind only one copy of Rev1, revealing an unexpected Rev1/Polζ architecture. In cells, mutation of the Rev7 dimer interface increases sensitivity to DNA damage. These results provide insights into the structure of the Rev1/Polζ TLS assembly and highlight the function of Rev7 homo- and heterodimerization. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
-Data source
SASBDB page | ![]() |
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-Related structure data
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External links
Related items in Molecule of the Month |
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-Models
Model #1625 | ![]() Type: atomic / Radius of dummy atoms: 1.90 A Comment: residues at N- and C-termini that were missing in PDB were built in extended conformation Chi-square value: 25.1295213698 ![]() |
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Sample
![]() | Name: Human Rev7 dimer in complex with Rev3 peptide @ 10.6 mg/mL Specimen concentration: 10.6 mg/ml / Entity id: 857 / 858 / 859 |
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Buffer | Name: 20 mM HEPES, 10 mM DTT, 5% glycerol / pH: 8 |
Entity #857 | Name: hRev7-WT dimer / Type: protein Description: Mitotic spindle assembly checkpoint protein MAD2B Formula weight: 24.391 / Num. of mol.: 2 / Source: Homo sapiens / References: UniProt: Q9UI95 Sequence: GMTTLTRQDL NFGQVVADVL CEFLEVAVHL ILYVREVYPV GIFQKRKKYN VPVQMSCHPE LNQYIQDTLH CVKPLLEKND VEKVVVVILD KEHRPVEKFV FEITQPPLLS ISSDSLLSHV EQLLRAFILK ISVCDAVLDH NPPGCTFTVL VHTREAATRN MEKIQVIKDF ...Sequence: GMTTLTRQDL NFGQVVADVL CEFLEVAVHL ILYVREVYPV GIFQKRKKYN VPVQMSCHPE LNQYIQDTLH CVKPLLEKND VEKVVVVILD KEHRPVEKFV FEITQPPLLS ISSDSLLSHV EQLLRAFILK ISVCDAVLDH NPPGCTFTVL VHTREAATRN MEKIQVIKDF PWILADEQDV HMHDPRLIPL KTMTSDILKM QLYVEERAHK GS |
Entity #858 | Name: Rev3-RBM2 / Type: protein / Description: DNA polymerase zeta catalytic subunit / Formula weight: 3.273 / Num. of mol.: 1 / Source: Homo sapiens / References: UniProt: O60673 Sequence: MEDKKIVIMP CKCAPSRQLV QVWLQAKE |
Entity #859 | Name: Rev3-RBM2 / Type: protein / Description: DNA polymerase zeta catalytic subunit / Formula weight: 3.273 / Num. of mol.: 1 / Source: Homo sapiens / References: UniProt: O60673 Sequence: MEDKKIVIMP CKCAPSRQLV QVWLQAKE |
-Experimental information
Beam | Instrument name: Cornell High Energy Synchrotron Source (CHESS) G1 City: Ithaca, NY / 国: USA ![]() ![]() | |||||||||||||||||||||||||||||||||||||||
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Detector | Name: Finger Lakes CCD / Type: CCD | |||||||||||||||||||||||||||||||||||||||
Scan | Measurement date: May 14, 2016 / Storage temperature: 4 °C / Cell temperature: 4 °C / Exposure time: 1 sec. / Number of frames: 10 / Unit: 1/A /
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Distance distribution function P(R) |
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Result | Comments: Model was created by mapping the dimer interface by mutagenesis (9 residues identified) and then docking the dimer with HADDOCK and the mutations. SAXS/WAXS was used for cross-validation.
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