+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-31765 | ||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Title | CryoEM structure of DDB1-VprBP complex in ARM-up conformation | ||||||||||||||||||
Map data | |||||||||||||||||||
Sample |
| ||||||||||||||||||
Function / homology | Function and homology information histone H2AT120 kinase activity / cell competition in a multicellular organism / positive regulation by virus of viral protein levels in host cell / V(D)J recombination / epigenetic programming in the zygotic pronuclei / spindle assembly involved in female meiosis / Cul4-RING E3 ubiquitin ligase complex / UV-damage excision repair / biological process involved in interaction with symbiont / regulation of mitotic cell cycle phase transition ...histone H2AT120 kinase activity / cell competition in a multicellular organism / positive regulation by virus of viral protein levels in host cell / V(D)J recombination / epigenetic programming in the zygotic pronuclei / spindle assembly involved in female meiosis / Cul4-RING E3 ubiquitin ligase complex / UV-damage excision repair / biological process involved in interaction with symbiont / regulation of mitotic cell cycle phase transition / WD40-repeat domain binding / Cul4A-RING E3 ubiquitin ligase complex / Cul4B-RING E3 ubiquitin ligase complex / ubiquitin ligase complex scaffold activity / negative regulation of reproductive process / negative regulation of developmental process / cullin family protein binding / ubiquitin-like ligase-substrate adaptor activity / viral release from host cell / ectopic germ cell programmed cell death / positive regulation of viral genome replication / positive regulation of gluconeogenesis / post-translational protein modification / B cell differentiation / proteasomal protein catabolic process / nuclear estrogen receptor binding / nucleotide-excision repair / Recognition of DNA damage by PCNA-containing replication complex / DNA Damage Recognition in GG-NER / regulation of circadian rhythm / Dual Incision in GG-NER / Transcription-Coupled Nucleotide Excision Repair (TC-NER) / Formation of TC-NER Pre-Incision Complex / fibrillar center / Wnt signaling pathway / Formation of Incision Complex in GG-NER / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / positive regulation of protein catabolic process / cellular response to UV / rhythmic process / protein-macromolecule adaptor activity / Antigen processing: Ubiquitination & Proteasome degradation / site of double-strand break / Neddylation / ubiquitin-dependent protein catabolic process / proteasome-mediated ubiquitin-dependent protein catabolic process / chromosome, telomeric region / damaged DNA binding / protein ubiquitination / non-specific serine/threonine protein kinase / phosphorylation / protein serine kinase activity / DNA repair / apoptotic process / DNA damage response / protein-containing complex binding / nucleolus / negative regulation of apoptotic process / negative regulation of transcription by RNA polymerase II / protein-containing complex / DNA binding / extracellular space / extracellular exosome / nucleoplasm / ATP binding / nucleus / cytoplasm Similarity search - Function | ||||||||||||||||||
Biological species | Homo sapiens (human) | ||||||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.2 Å | ||||||||||||||||||
Authors | Wang D / Xu J / Liu Q / Xiang Y | ||||||||||||||||||
Funding support | China, 5 items
| ||||||||||||||||||
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 |
|
-Structure visualization
Supplemental images |
---|
-Downloads & links
-EMDB archive
Map data | emd_31765.map.gz | 84.3 MB | EMDB map data format | |
---|---|---|---|---|
Header (meta data) | emd-31765-v30.xml emd-31765.xml | 14.2 KB 14.2 KB | Display Display | EMDB header |
Images | emd_31765.png | 124.5 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-31765 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-31765 | HTTPS FTP |
-Related structure data
Related structure data | 7v7bMC 7v7cC M: atomic model generated by this map C: citing same article (ref.) |
---|---|
Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
---|---|
Related items in Molecule of the Month |
-Map
File | Download / File: emd_31765.map.gz / Format: CCP4 / Size: 91.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Voxel size | X=Y=Z: 1.091 Å | ||||||||||||||||||||
Density |
| ||||||||||||||||||||
Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
|
-Supplemental data
-Sample components
-Entire : CryoEM structure of DDB1-VprBP complex in "ARM-up" conformation
Entire | Name: CryoEM structure of DDB1-VprBP complex in "ARM-up" conformation |
---|---|
Components |
|
-Supramolecule #1: CryoEM structure of DDB1-VprBP complex in "ARM-up" conformation
Supramolecule | Name: CryoEM structure of DDB1-VprBP complex in "ARM-up" conformation type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
---|---|
Source (natural) | Organism: Homo sapiens (human) |
Recombinant expression | Organism: Trichoplusia ni (cabbage looper) |
-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 |
---|---|
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 |
---|---|
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 |
-Experimental details
-Structure determination
Method | cryo EM |
---|---|
Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.5 |
---|---|
Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
---|---|
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy |
Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 50.0 e/Å2 |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
CTF correction | Software - Name: CTFFIND |
---|---|
Initial angle assignment | Type: MAXIMUM LIKELIHOOD / Software - Name: RELION |
Final angle assignment | Type: MAXIMUM LIKELIHOOD / Software - Name: RELION |
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 4.2 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION / Number images used: 84405 |
-Atomic model buiding 1
Refinement | Space: REAL / Protocol: RIGID BODY FIT |
---|---|
Output model | PDB-7v7b: |