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- SASDCT8: Uncharacterized protein CTHT_0072540 (Core) from Chaetomium therm... -
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Open data
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Basic information
Entry | Database: SASBDB / ID: SASDCT8 |
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![]() | Uncharacterized protein CTHT_0072540 (Core) from Chaetomium thermophilum
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Function / homology | ![]() Prp19 complex / U2-type catalytic step 1 spliceosome / protein K63-linked ubiquitination / RING-type E3 ubiquitin transferase / mRNA splicing, via spliceosome / ubiquitin protein ligase activity / DNA repair / cytoplasm Similarity search - Function |
Biological species | ![]() |
![]() | ![]() Title: Prp19/Pso4 Is an Autoinhibited Ubiquitin Ligase Activated by Stepwise Assembly of Three Splicing Factors. Authors: Tales Rocha de Moura / Sina Mozaffari-Jovin / Csaba Zoltán Kibédi Szabó / Jana Schmitzová / Olexandr Dybkov / Constantin Cretu / Michael Kachala / Dmitri Svergun / Henning Urlaub / ...Authors: Tales Rocha de Moura / Sina Mozaffari-Jovin / Csaba Zoltán Kibédi Szabó / Jana Schmitzová / Olexandr Dybkov / Constantin Cretu / Michael Kachala / Dmitri Svergun / Henning Urlaub / Reinhard Lührmann / Vladimir Pena / ![]() Abstract: Human nineteen complex (NTC) acts as a multimeric E3 ubiquitin ligase in DNA repair and splicing. The transfer of ubiquitin is mediated by Prp19-a homotetrameric component of NTC whose elongated ...Human nineteen complex (NTC) acts as a multimeric E3 ubiquitin ligase in DNA repair and splicing. The transfer of ubiquitin is mediated by Prp19-a homotetrameric component of NTC whose elongated coiled coils serve as an assembly axis for two other proteins called SPF27 and CDC5L. We find that Prp19 is inactive on its own and have elucidated the structural basis of its autoinhibition by crystallography and mutational analysis. Formation of the NTC core by stepwise assembly of SPF27, CDC5L, and PLRG1 onto the Prp19 tetramer enables ubiquitin ligation. Protein-protein crosslinking of NTC, functional assays in vitro, and assessment of its role in DNA damage response provide mechanistic insight into the organization of the NTC core and the communication between PLRG1 and Prp19 that enables E3 activity. This reveals a unique mode of regulation for a complex E3 ligase and advances understanding of its dynamics in various cellular pathways. |
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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 #1379 | ![]() Type: dummy / Radius of dummy atoms: 2.75 A / Chi-square value: 1.041 ![]() |
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Model #1380 | ![]() Type: atomic / Radius of dummy atoms: 1.90 A / Chi-square value: 1.475 ![]() |
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Sample
![]() | Name: Uncharacterized protein CTHT_0072540 (Core) from Chaetomium thermophilum Specimen concentration: 1.30-5.00 |
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Buffer | Name: 20 mM HEPES, 100 mM NaCl, 2 mM β-mercaptoethanol / pH: 7.5 |
Entity #762 | Type: protein / Description: hypothetical protein CTHT_0072540 / Formula weight: 15.552 / Num. of mol.: 4 / Source: Chaetomium thermophilum / References: UniProt: G0SFY0 Sequence: MLCALSGEIP EEPVVSKKTG VLFEKRLILK YLEEHNNIEP GTTEELDPET DLLPIKTSRV VRPRPPNFTS IPSLLKAFQD EWDALVLETY TTREQLARVR EELATALYQH DAAVRVIARL TRERDEAREA LARLTV |
-Experimental information
Beam | Instrument name: PETRA III P12 / City: Hamburg / 国: Germany ![]() | |||||||||||||||||||||||||||||||||||||||
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Detector | Name: Pilatus 2M | |||||||||||||||||||||||||||||||||||||||
Scan | Measurement date: Jul 30, 2013 / Cell temperature: 25 °C / Exposure time: 1 sec. / Number of frames: 20 / Unit: 1/nm /
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Distance distribution function P(R) |
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Result |
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