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Yorodumi- SASDCV8: Uncharacterized protein CTHT_0072540 (Prp19 full-length) from Cha... -
+Open data
-Basic information
Entry | Database: SASBDB / ID: SASDCV8 |
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Sample | Uncharacterized protein CTHT_0072540 (Prp19 full-length) from Chaetomium thermophilum
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Function / homology | Function and homology information Prp19 complex / protein K63-linked ubiquitination / spliceosomal complex / RING-type E3 ubiquitin transferase / mRNA splicing, via spliceosome / ubiquitin protein ligase activity / DNA repair Similarity search - Function |
Biological species | Chaetomium thermophilum (fungus) |
Citation | Journal: Mol Cell / Year: 2018 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. |
Contact author |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Data source
SASBDB page | SASDCV8 |
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-Related structure data
-External links
Related items in Molecule of the Month |
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-Models
Model #1468 | Type: atomic / Radius of dummy atoms: 1.90 A / Chi-square value: 1.555 Search similar-shape structures of this assembly by Omokage search (details) |
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Model #1469 | Type: dummy / Software: (r9988) / Radius of dummy atoms: 3.60 A / Chi-square value: 1.003 / P-value: 0.030000 Search similar-shape structures of this assembly by Omokage search (details) |
-Sample
Sample | Name: Uncharacterized protein CTHT_0072540 (Prp19 full-length) from Chaetomium thermophilum Specimen concentration: 0.60-4.40 |
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Buffer | Name: 20 mM HEPES, 100 mM NaCl, 2 mM β-mercaptoethanol / pH: 7.5 |
Entity #763 | Type: protein / Description: Full-length hypothetical protein CTHT_0072540 / Formula weight: 51.788 / Num. of mol.: 4 / Source: Chaetomium thermophilum / References: UniProt: G0SFY0 Sequence: MLCALSGEIP EEPVVSKKTG VLFEKRLILK YLEEHNNIEP GTTEELDPET DLLPIKTSRV VRPRPPNFTS IPSLLKAFQD EWDALVLETY TTREQLARVR EELATALYQH DAAVRVIARL TRERDEAREA LARLTVTGAA PAAQNGEAMA VDSESLSEGL VEHVNEVQQQ ...Sequence: MLCALSGEIP EEPVVSKKTG VLFEKRLILK YLEEHNNIEP GTTEELDPET DLLPIKTSRV VRPRPPNFTS IPSLLKAFQD EWDALVLETY TTREQLARVR EELATALYQH DAAVRVIARL TRERDEAREA LARLTVTGAA PAAQNGEAMA VDSESLSEGL VEHVNEVQQQ LMKTRKKRPI PQGWATADDV AALQQVAYTD LNVTQASSLD LENECAAVGG LDGKLDIYSV VANKVERTLD IGEPVTATEW TGTKVVIGTA KGWVKVYDAG RESATFQTHA GPVTGLAVHP GGRILASVGV DKSFVFYDLE TGERVARGYA DAALTTCAFH PDGNLFAAGT QTGHILVFHT TTLEQAESFP LGTPIQALAF SENGFWFAAT GKGTSSVTIF DLRKSGAAAA VKELQTGEVL SISWDYTGQY LATGGGTGVT VQMYTKATKS WSEPVRLGMP VVGVKWGGEA KRLVVVSREG VVSVLGKKEE |
-Experimental information
Beam | Instrument name: MAX IV I911-4 / City: Lund / 国: Sweden / Type of source: X-ray synchrotron / Wavelength: 0.091 Å / Dist. spec. to detc.: 2.2 mm | |||||||||||||||||||||||||||||||||||||||
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Detector | Name: Pilatus 1M / Type: Dectris / Pixsize x: 172 mm | |||||||||||||||||||||||||||||||||||||||
Scan | Title: Uncharacterized protein CTHT_0072540 (Prp19 full-length) from Chaetomium thermophilum Measurement date: Oct 15, 2013 / Cell temperature: 25 °C / Exposure time: 120 sec. / Unit: 1/nm /
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Distance distribution function P(R) | Sofotware P(R): GNOM 4.6 / Number of points: 263 /
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Result | Type of curve: merged
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