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Open data
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Basic information
Entry | Database: SASBDB / ID: SASDED6 |
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![]() | Proliferating cell nuclear antigen - UbPCNA - Split Fusion Trimer
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Function / homology | ![]() Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha) / meiotic mismatch repair / Processive synthesis on the lagging strand / Removal of the Flap Intermediate / E3 ubiquitin ligases ubiquitinate target proteins / Polymerase switching / SUMOylation of DNA replication proteins / positive regulation of DNA metabolic process / maintenance of DNA trinucleotide repeats / Translesion Synthesis by POLH ...Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha) / meiotic mismatch repair / Processive synthesis on the lagging strand / Removal of the Flap Intermediate / E3 ubiquitin ligases ubiquitinate target proteins / Polymerase switching / SUMOylation of DNA replication proteins / positive regulation of DNA metabolic process / maintenance of DNA trinucleotide repeats / Translesion Synthesis by POLH / Translesion synthesis by REV1 / Translesion synthesis by POLK / Translesion synthesis by POLI / establishment of mitotic sister chromatid cohesion / PCNA complex / Termination of translesion DNA synthesis / lagging strand elongation / postreplication repair / silent mating-type cassette heterochromatin formation / mitotic sister chromatid cohesion / error-free translesion synthesis / DNA polymerase processivity factor activity / leading strand elongation / Dual incision in TC-NER / subtelomeric heterochromatin formation / mismatch repair / translesion synthesis / positive regulation of DNA repair / replication fork / positive regulation of DNA replication / nucleotide-excision repair / mitotic cell cycle / chromosome, telomeric region / DNA binding / identical protein binding / nucleus Similarity search - Function |
Biological species | ![]() ![]() |
![]() | ![]() Title: Conformational Flexibility of Ubiquitin-Modified and SUMO-Modified PCNA Shown by Full-Ensemble Hybrid Methods. Authors: Kyle T Powers / Emily D Lavering / M Todd Washington / ![]() Abstract: Ubiquitin-modified proliferating cell nuclear antigen (PCNA) and small ubiquitin-like modifier (SUMO)-modified PCNA regulate DNA damage tolerance pathways. X-ray crystal structures of these proteins ...Ubiquitin-modified proliferating cell nuclear antigen (PCNA) and small ubiquitin-like modifier (SUMO)-modified PCNA regulate DNA damage tolerance pathways. X-ray crystal structures of these proteins suggested that they do not have much conformational flexibility because the modifiers have preferred binding sites on the surface of PCNA. By contrast, small-angle X-ray scattering analyses of these proteins suggested that they have different degrees of conformational flexibility, with SUMO-modified PCNA being more flexible. These conclusions were based on minimal-ensemble hybrid approaches, which produce unrealistic models by representing flexible proteins with only a few static structures. To overcome the limitations of minimal-ensemble hybrid approaches and to determine the degree of conformational flexibility of ubiquitin-modified PCNA and SUMO-modified PCNA, we utilized a novel full-ensemble hybrid approach. We carried out molecular simulations and small-angle X-ray scattering analyses of both proteins and obtained outstanding agreement between the full ensembles generated by the simulations and the experimental data. We found that both proteins have a high degree of conformational flexibility. The modifiers occupy many positions around the back and side of the PCNA ring. Moreover, we found no preferred ubiquitin-binding or SUMO-binding sites on PCNA. This conformational flexibility likely facilitates the recognition of downstream effector proteins and the formation of PCNA tool belts. |
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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
Related structure data | C: citing same article ( |
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Similar structure data |
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External links
Related items in Molecule of the Month |
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-Models
Model #2532 | ![]() Type: other / Comment: One representative PDB from the simulation. / Chi-square value: 2.650 ![]() |
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Sample
![]() | Name: Proliferating cell nuclear antigen - UbPCNA - Split Fusion Trimer Specimen concentration: 20.7 mg/ml |
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Buffer | Name: 20 mM Tris, 150 mM NaCl, 5% glycerol, 1 mM TCEP / pH: 7.5 / Comment: Room temperature |
Entity #1328 | Name: PCNA / Type: protein / Description: Proliferating cell nuclear antigen / Formula weight: 39.101 / Num. of mol.: 3 Source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) References: UniProt: P15873 Sequence: MGSSHHHHHH SQDPMQIFVK TLTGKTITLE VEPSDTIENV KAKIQDKEGI PPDQQRLIFA GKQLEDGRTL SDYNIQKEST LHLVLRLRGG PGETIKFVAD GDIGSGSVII KPFVDMEHPE TSIKLEMDQP VDLTFGAKYL LDIIKGSSLS DRVGIRLSSE APALFQFDLK ...Sequence: MGSSHHHHHH SQDPMQIFVK TLTGKTITLE VEPSDTIENV KAKIQDKEGI PPDQQRLIFA GKQLEDGRTL SDYNIQKEST LHLVLRLRGG PGETIKFVAD GDIGSGSVII KPFVDMEHPE TSIKLEMDQP VDLTFGAKYL LDIIKGSSLS DRVGIRLSSE APALFQFDLK SGFLQFFLAP KFNDEEMLEA KFEEASLFKR IIDGFKDCVQ LVNFQCKEDG IIAQAVDDSR VLLVSLEIGV EAFQEYRCDH PVTLGMDLTS LSKILRCGNN TDTLTLIADN TPDSIILLFE DTKKDRIAEY SLKLMDIDAD FLKIEELQYD STLSLPSSEF SKIVRDLSQL SDSINIMIT |
-Experimental information
Beam | Instrument name: Advanced Photon Source (APS), Argonne National Laboratory BioCAT 18ID City: Lemont, IL / 国: USA ![]() | ||||||||||||||||||||||||||||||
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Detector | Name: Pilatus3 X 1M / Pixsize x: 0.172 mm | ||||||||||||||||||||||||||||||
Scan | Measurement date: Aug 6, 2018 / Storage temperature: 22 °C / Cell temperature: 22 °C / Exposure time: 0.5 sec. / Number of frames: 320 / Unit: 1/A /
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Distance distribution function P(R) |
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Result |
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