+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-31766 | ||||||||||||||||||
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Title | CryoEM structure of DDB1-VprBP-Vpr-UNG2(94-313) complex | ||||||||||||||||||
Map data | |||||||||||||||||||
Sample |
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Function / homology | Function and homology information : / histone H2AT120 kinase activity / cell competition in a multicellular organism / symbiont-mediated arrest of host cell cycle during G2/M transition / base-excision repair, AP site formation via deaminated base removal / uracil-DNA glycosylase / depyrimidination / Displacement of DNA glycosylase by APEX1 / V(D)J recombination / positive regulation by virus of viral protein levels in host cell ...: / histone H2AT120 kinase activity / cell competition in a multicellular organism / symbiont-mediated arrest of host cell cycle during G2/M transition / base-excision repair, AP site formation via deaminated base removal / uracil-DNA glycosylase / depyrimidination / Displacement of DNA glycosylase by APEX1 / V(D)J recombination / positive regulation by virus of viral protein levels in host cell / epigenetic programming in the zygotic pronuclei / isotype switching / spindle assembly involved in female meiosis / Cul4-RING E3 ubiquitin ligase complex / UV-damage excision repair / uracil DNA N-glycosylase activity / biological process involved in interaction with symbiont / regulation of mitotic cell cycle phase transition / Cul4A-RING E3 ubiquitin ligase complex / WD40-repeat domain binding / ubiquitin ligase complex scaffold activity / Cul4B-RING E3 ubiquitin ligase complex / negative regulation of reproductive process / negative regulation of developmental process / cullin family protein binding / ribosomal small subunit binding / viral release from host cell / ubiquitin-like ligase-substrate adaptor activity / ectopic germ cell programmed cell death / proteasomal protein catabolic process / somatic hypermutation of immunoglobulin genes / positive regulation of viral genome replication / monoatomic ion transport / positive regulation of gluconeogenesis / Recognition and association of DNA glycosylase with site containing an affected pyrimidine / Cleavage of the damaged pyrimidine / B cell differentiation / post-translational protein modification / Chromatin modifications during the maternal to zygotic transition (MZT) / virion component / nuclear estrogen receptor binding / nucleotide-excision repair / Recognition of DNA damage by PCNA-containing replication complex / DNA Damage Recognition in GG-NER / cell cycle / base-excision repair / protein homooligomerization / regulation of circadian rhythm / Transcription-Coupled Nucleotide Excision Repair (TC-NER) / Formation of TC-NER Pre-Incision Complex / Dual Incision in GG-NER / Wnt signaling pathway / fibrillar center / Formation of Incision Complex in GG-NER / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / viral penetration into host nucleus / positive regulation of protein catabolic process / cellular response to UV / rhythmic process / Antigen processing: Ubiquitination & Proteasome degradation / Neddylation / protein-macromolecule adaptor activity / site of double-strand break / ubiquitin-dependent protein catabolic process / proteasome-mediated ubiquitin-dependent protein catabolic process / host extracellular space / damaged DNA binding / chromosome, telomeric region / non-specific serine/threonine protein kinase / protein ubiquitination / symbiont entry into host cell / DNA repair / protein serine kinase activity / DNA-templated transcription / DNA damage response / host cell nucleus / regulation of DNA-templated transcription / protein-containing complex binding / apoptotic process / nucleolus / negative regulation of apoptotic process / negative regulation of transcription by RNA polymerase II / protein-containing complex / mitochondrion / DNA binding / extracellular space / extracellular exosome / nucleoplasm / ATP binding / nucleus / cytoplasm Similarity search - Function | ||||||||||||||||||
Biological species | Homo sapiens (human) / Human immunodeficiency virus 1 | ||||||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.7 Å | ||||||||||||||||||
Authors | Wang D / Xu J / Liu Q / Xiang Y | ||||||||||||||||||
Funding support | China, 5 items
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Citation | Journal: To Be Published Title: Structural insights into the HIV-1 Vpr mediated ubiquitination through the Cullin-RING E3 ubiquitin ligase Authors: Wang D / Xu J / Liu Q / Xiang Y | ||||||||||||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_31766.map.gz | 111.5 MB | EMDB map data format | |
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Header (meta data) | emd-31766-v30.xml emd-31766.xml | 16.4 KB 16.4 KB | Display Display | EMDB header |
Images | emd_31766.png | 118.7 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-31766 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-31766 | HTTPS FTP |
-Related structure data
Related structure data | 7v7cMC 7v7bC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_31766.map.gz / Format: CCP4 / Size: 125 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||
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Voxel size | X=Y=Z: 1.0742 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Sample components
-Entire : DDB1-VprBP-Vpr-UNG2(94-313) complex
Entire | Name: DDB1-VprBP-Vpr-UNG2(94-313) complex |
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Components |
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-Supramolecule #1: DDB1-VprBP-Vpr-UNG2(94-313) complex
Supramolecule | Name: DDB1-VprBP-Vpr-UNG2(94-313) complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: Homo sapiens (human) |
Recombinant expression | Organism: Trichoplusia ni (cabbage looper) |
Molecular weight | Theoretical: 0.66 kDa/nm |
-Macromolecule #1: DDB1- and CUL4-associated factor 1
Macromolecule | Name: DDB1- and CUL4-associated factor 1 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO / EC number: non-specific serine/threonine protein kinase |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 169.194781 KDa |
Recombinant expression | Organism: Trichoplusia ni (cabbage looper) |
Sequence | String: MTTVVVHVDS KAELTTLLEQ WEKEHGSGQD MVPILTRMSQ LIEKETEEYR KGDPDPFDDR HPGRADPECM LGHLLRILFK NDDFMNALV NAYVMTSREP PLNTAACRLL LDIMPGLETA VVFQEKEGIV ENLFKWAREA DQPLRTYSTG LLGGAMENQD I AANYRDEN ...String: MTTVVVHVDS KAELTTLLEQ WEKEHGSGQD MVPILTRMSQ LIEKETEEYR KGDPDPFDDR HPGRADPECM LGHLLRILFK NDDFMNALV NAYVMTSREP PLNTAACRLL LDIMPGLETA VVFQEKEGIV ENLFKWAREA DQPLRTYSTG LLGGAMENQD I AANYRDEN SQLVAIVLRR LRELQLQEVA LRQENKRPSP RKLSSEPLLP LDEEAVDMDY GDMAVDVVDG DQEEASGDME IS FHLDSGH KTSSRVNSTT KPEDGGLKKN KSAKQGDREN FRKAKQKLGF SSSDPDRMFV ELSNSSWSEM SPWVIGTNYT LYP MTPAIE QRLILQYLTP LGEYQELLPI FMQLGSRELM MFYIDLKQTN DVLLTFEALK HLASLLLHNK FATEFVAHGG VQKL LEIPR PSMAATGVSM CLYYLSYNQD AMERVCMHPH NVLSDVVNYT LWLMECSHAS GCCHATMFFS ICFSFRAVLE LFDRY DGLR RLVNLISTLE ILNLEDQGAL LSDDEIFASR QTGKHTCMAL RKYFEAHLAI KLEQVKQSLQ RTEGGILVHP QPPYKA CSY THEQIVEMME FLIEYGPAQL YWEPAEVFLK LSCVQLLLQL ISIACNWKTY YARNDTVRFA LDVLAILTVV PKIQLQL AE SVDVLDEAGS TVSTVGISII LGVAEGEFFI HDAEIQKSAL QIIINCVCGP DNRISSIGKF ISGTPRRKLP QNPKSSEH T LAKMWNVVQS NNGIKVLLSL LSIKMPITDA DQIRALACKA LVGLSRSSTV RQIISKLPLF SSCQIQQLMK EPVLQDKRS DHVKFCKYAA ELIERVSGKP LLIGTDVSLA RLQKADVVAQ SRISFPEKEL LLLIRNHLIS KGLGETATVL TKEADLPMTA ASHSSAFTP VTAAASPVSL PRTPRIANGI ATRLGSHAAV GASAPSAPTA HPQPRPPQGP LALPGPSYAG NSPLIGRISF I RERPSPCN GRKIRVLRQK SDHGAYSQSP AIKKQLDRHL PSPPTLDSII TEYLREQHAR CKNPVATCPP FSLFTPHQCP EP KQRRQAP INFTSRLNRR ASFPKYGGVD GGCFDRHLIF SRFRPISVFR EANEDESGFT CCAFSARERF LMLGTCTGQL KLY NVFSGQ EEASYNCHNS AITHLEPSRD GSLLLTSATW SQPLSALWGM KSVFDMKHSF TEDHYVEFSK HSQDRVIGTK GDIA HIYDI QTGNKLLTLF NPDLANNYKR NCATFNPTDD LVLNDGVLWD VRSAQAIHKF DKFNMNISGV FHPNGLEVII NTEIW DLRT FHLLHTVPAL DQCRVVFNHT GTVMYGAMLQ ADDEDDLMEE RMKSPFGSSF RTFNATDYKP IATIDVKRNI FDLCTD TKD CYLAVIENQG SMDALNMDTV CRLYEVGRQR LAEDEDEEED QEEEEQEEED DDEDDDDTDD LDELDTDQLL EAELEED DN NENAGEDGDN DFSPSDEELA NLLEEGEDGE DEDSDADEEV ELILGDTDSS DNSDLEDDII LSLNE |
-Macromolecule #2: DNA damage-binding protein 1
Macromolecule | Name: DNA damage-binding protein 1 / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 127.097469 KDa |
Recombinant expression | Organism: Trichoplusia ni (cabbage looper) |
Sequence | String: MSYNYVVTAQ KPTAVNGCVT GHFTSAEDLN LLIAKNTRLE IYVVTAEGLR PVKEVGMYGK IAVMELFRPK GESKDLLFIL TAKYNACIL EYKQSGESID IITRAHGNVQ DRIGRPSETG IIGIIDPECR MIGLRLYDGL FKVIPLDRDN KELKAFNIRL E ELHVIDVK ...String: MSYNYVVTAQ KPTAVNGCVT GHFTSAEDLN LLIAKNTRLE IYVVTAEGLR PVKEVGMYGK IAVMELFRPK GESKDLLFIL TAKYNACIL EYKQSGESID IITRAHGNVQ DRIGRPSETG IIGIIDPECR MIGLRLYDGL FKVIPLDRDN KELKAFNIRL E ELHVIDVK FLYGCQAPTI CFVYQDPQGR HVKTYEVSLR EKEFNKGPWK QENVEAEASM VIAVPEPFGG AIIIGQESIT YH NGDKYLA IAPPIIKQST IVCHNRVDPN GSRYLLGDME GRLFMLLLEK EEQMDGTVTL KDLRVELLGE TSIAECLTYL DNG VVFVGS RLGDSQLVKL NVDSNEQGSY VVAMETFTNL GPIVDMCVVD LERQGQGQLV TCSGAFKEGS LRIIRNGIGI HEHA SIDLP GIKGLWPLRS DPNRETDDTL VLSFVGQTRV LMLNGEEVEE TELMGFVDDQ QTFFCGNVAH QQLIQITSAS VRLVS QEPK ALVSEWKEPQ AKNISVASCN SSQVVVAVGR ALYYLQIHPQ ELRQISHTEM EHEVACLDIT PLGDSNGLSP LCAIGL WTD ISARILKLPS FELLHKEMLG GEIIPRSILM TTFESSHYLL CALGDGALFY FGLNIETGLL SDRKKVTLGT QPTVLRT FR SLSTTNVFAC SDRPTVIYSS NHKLVFSNVN LKEVNYMCPL NSDGYPDSLA LANNSTLTIG TIDEIQKLHI RTVPLYES P RKICYQEVSQ CFGVLSSRIE VQDTSGGTTA LRPSASTQAL SSSVSSSKLF SSSTAPHETS FGEEVEVHNL LIIDQHTFE VLHAHQFLQN EYALSLVSCK LGKDPNTYFI VGTAMVYPEE AEPKQGRIVV FQYSDGKLQT VAEKEVKGAV YSMVEFNGKL LASINSTVR LYEWTTEKEL RTECNHYNNI MALYLKTKGD FILVGDLMRS VLLLAYKPME GNFEEIARDF NPNWMSAVEI L DDDNFLGA ENAFNLFVCQ KDSAATTDEE RQHLQEVGLF HLGEFVNVFC HGSLVMQNLG ETSTPTQGSV LFGTVNGMIG LV TSLSESW YNLLLDMQNR LNKVIKSVGK IEHSFWRSFH TERKTEPATG FIDGDLIESF LDISRPKMQE VVANLQYDDG SGM KREATA DDLIKVVEEL TRIH |
-Macromolecule #3: Protein Vpr
Macromolecule | Name: Protein Vpr / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: Human immunodeficiency virus 1 |
Molecular weight | Theoretical: 11.396878 KDa |
Recombinant expression | Organism: Escherichia coli (E. coli) |
Sequence | String: MEQAPEDQGP QREPYNEWTL ELLEELKSEA VRHFPRIWLH NLGQHIYETY GDTWAGVEAI IRILQQLLFI HFRIGCRHSR IGVTRQRRA RNGASRS |
-Macromolecule #4: Uracil-DNA glycosylase
Macromolecule | Name: Uracil-DNA glycosylase / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO / EC number: uracil-DNA glycosylase |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 25.136654 KDa |
Recombinant expression | Organism: Escherichia coli (E. coli) |
Sequence | String: FGESWKKHLS GEFGKPYFIK LMGFVAEERK HYTVYPPPHQ VFTWTQMCDI KDVKVVILGQ DPYHGPNQAH GLCFSVQRPV PPPPSLENI YKELSTDIED FVHPGHGDLS GWAKQGVLLL NAVLTVRAHQ ANSHKERGWE QFTDAVVSWL NQNSNGLVFL L WGSYAQKK ...String: FGESWKKHLS GEFGKPYFIK LMGFVAEERK HYTVYPPPHQ VFTWTQMCDI KDVKVVILGQ DPYHGPNQAH GLCFSVQRPV PPPPSLENI YKELSTDIED FVHPGHGDLS GWAKQGVLLL NAVLTVRAHQ ANSHKERGWE QFTDAVVSWL NQNSNGLVFL L WGSYAQKK GSAIDRKRHH VLQTAHPSPL SVYRGFFGCR HFSKTNELLQ KSGKKPIDWK EL |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
CTF correction | Software - Name: CTFFIND |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.7 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION / Number images used: 145568 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD / Software - Name: RELION |
Final angle assignment | Type: MAXIMUM LIKELIHOOD / Software - Name: RELION |
-Atomic model buiding 1
Refinement | Protocol: RIGID BODY FIT |
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Output model | PDB-7v7c: |