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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | ASFV RNA polymerase-M1249L complex4 | |||||||||
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![]() | ASFV / RNA polymerase / VIRAL PROTEIN | |||||||||
Function / homology | ![]() viral transcription / DNA-directed RNA polymerase complex / : / : / : / : / : / : / DNA-directed RNA polymerase / DNA binding Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.97 Å | |||||||||
![]() | Feng XY | |||||||||
Funding support | 1 items
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![]() | ![]() Title: Transcription regulation of African swine fever virus: dual role of M1249L. Authors: Dongming Zhao / Nan Wang / Xiaoying Feng / Zhenjiang Zhang / Kongen Xu / Tao Zheng / Yunge Yang / Xuemei Li / Xianjin Ou / Rui Zhao / Zihe Rao / Zhigao Bu / Yutao Chen / Xiangxi Wang / ![]() Abstract: African swine fever virus (ASFV), which poses significant risks to the global economy, encodes a unique host-independent transcription system. This system comprises an eight-subunit RNA polymerase ...African swine fever virus (ASFV), which poses significant risks to the global economy, encodes a unique host-independent transcription system. This system comprises an eight-subunit RNA polymerase (vRNAP), temporally expressed transcription factors and transcript associated proteins, facilitating cross-species transmission via intermediate host. The protein composition of the virion and the presence of transcription factors in virus genome suggest existence of distinct transcription systems during viral infection. However, the precise mechanisms of transcription regulation remain elusive. Through analyses of dynamic transcriptome, vRNAP-associated components and cell-based assay, the critical role of M1249L in viral transcription regulation has been highlighted. Atomic-resolution structures of vRNAP-M1249L supercomplex, exhibiting a variety of conformations, have uncovered the dual functions of M1249L. During early transcription, M1249L could serve as multiple temporary transcription factors with C-terminal domain acting as a switcher for activation/inactivation, while during late transcription it aids in the packaging of the transcription machinery. The structural and functional characteristics of M1249L underscore its vital roles in ASFV transcription, packaging, and capsid assembly, presenting novel opportunities for therapeutic intervention. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 167.8 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 19.4 KB 19.4 KB | Display Display | ![]() |
Images | ![]() | 14.8 KB | ||
Filedesc metadata | ![]() | 7.3 KB | ||
Others | ![]() ![]() | 165.1 MB 165.1 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8yqxMC ![]() 8yqtC ![]() 8yquC ![]() 8yqvC ![]() 8yqwC ![]() 8yqyC ![]() 8yqzC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.808 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_39509_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_39509_half_map_2.map | ||||||||||||
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Sample components
-Entire : African swine fever virus RNA polymerase complex
Entire | Name: African swine fever virus RNA polymerase complex |
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Components |
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-Supramolecule #1: African swine fever virus RNA polymerase complex
Supramolecule | Name: African swine fever virus RNA polymerase complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: DNA-directed RNA polymerase subunit
Macromolecule | Name: DNA-directed RNA polymerase subunit / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: DNA-directed RNA polymerase |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 163.933938 KDa |
Sequence | String: MEAGYAEIAA VQFNIAGDND HKRQGVMEVT ISNLFEGTLP AEGGIYDARM GTTDHHYKCI TCSHQRKQCM GHPGILQMHA PVLQPLFIA EIRRWLRVIC LNCGAPIVDL KRYEHLIRPK RLIEAASSQT EGKQCYVCKA VHPKIVKDSE DYFTFWADQQ G KIDKLYPQ ...String: MEAGYAEIAA VQFNIAGDND HKRQGVMEVT ISNLFEGTLP AEGGIYDARM GTTDHHYKCI TCSHQRKQCM GHPGILQMHA PVLQPLFIA EIRRWLRVIC LNCGAPIVDL KRYEHLIRPK RLIEAASSQT EGKQCYVCKA VHPKIVKDSE DYFTFWADQQ G KIDKLYPQ IIREIFSRVT YDTVVKLGRS KNSHPEKLVL KAIQIPPISI RPGIRLGIGS GPQSFHDINN VIQYLVRKNL LI PKDLQIV RGQKIPLNID RNLQTIQQLY YNFLLDSVST TATQGGTGKR GIVMGARPAP SIMRRLPRKE GRIRKSLLGS QVW SISRST ICGNSDLHLD EVGYPISFAR TLQVAETVQH YNINRLMPYF LNGKRQYPGC SRVYKQITQS VHDIEGLKQD FRLE VGDIL YRDVVTGDVA FFNRQPSLER SSIGVHRIVV LENPKISTFQ MNVSACAWYN ADFDGDQMNL WVPWSVMSRV EAELL CSVR NWFISTKSSG PVNGQVQDST VGSFLLTRTN TPMGKNVMNK LHAMGLFQTT QTDPPCFANY SPTDLLDGKS VVSMLL RQT PINYQRAPTW YSEVYAPYMH YNKQDISTQI RNGELIEGVL DKKAVGAGSS GGIYHLISRR YGPQQALKMI FATQQLA LN YVRNAGFTVS TADMLLTPEA HQEVQEIINE LLLESEEINN RLLHGDIMPP IGLTTHDFYE KLQLNALKFP DRILKPIM N SINPETNGLF QMVATGAKGS NPNMIHIMAG IGQIEINTQR IQPQFSFGRT LVYYPRFALE AQAYGFICNS YIAGLTSPE FIFGEMNGRF DLINKALSTS STGYANRKAI FGLQSCIVDY YRRVSIDTRL VQQLYGEDGL DARQLETVRF ETIMLSDQEL EDKFKYTGI QSPLFEEEFS RLKKDRDKYR QIFLNVENFN FSQLLTDVRQ VPVNVASIVK NILLSSTSGV LPFDEKSILQ K YAMVKTFC KNLPYVFINN IQERLQTPIP VYLKRAASLM RMLIRIELAT VKTLNITCEQ MSAILDLIRL QYTQSLINYG EA VGILAAQ SVSEPLTQYM LDSHHRSVAG GTNKSGIVRP QEIFSAKPVE AEQSSEMLLR LKNPEVETNK TYAQEIANSI ELI TFERLI LQWHLLYETY SSTKKNVMYP DFASDVEWMT DFLENHPLLQ PPEDIANWCI RLELNKTTMI LKSISLESII NSLR AKHPN TYIMHSVENT ASGIPIIIRI YLRESAFRRS TNTRMATDEK IAVNVVDKLL NSTIRGIPGI KNANVVKLMR HRVDA QGKL VRLDNIYAIK TNGTNIFGAM LDDNIDPYTI VSSSIGDTME LYGIEAARQK IISEIRTVMG DKGPNHRHLL MYADLM TRT GQVTSLEKAG LNAREPSNVL LRMALSSPVQ VLTDAAVDSA VNPIYGIAAP TLMGSVPRIG TMYSDIIMDE KYITENY KS VDSLIDML UniProtKB: DNA-directed RNA polymerase subunit |
-Macromolecule #2: D339L
Macromolecule | Name: D339L / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 38.798594 KDa |
Sequence | String: MIDQKIFETT LNIDDPTNFC TNVEAHLLKE LENIYVGKCF KNSFILNITG VIQRSPCFIM RTNNSGRGYM HVRFSAVVSY LNAFDLIAA VKIIKNDSNI ILGESLLTEP VTIVIPSSES QNNVAEVGQI VPVQLANSSV YYIPGRQQAS ATGSIFIPKH T FSVYHVQE ...String: MIDQKIFETT LNIDDPTNFC TNVEAHLLKE LENIYVGKCF KNSFILNITG VIQRSPCFIM RTNNSGRGYM HVRFSAVVSY LNAFDLIAA VKIIKNDSNI ILGESLLTEP VTIVIPSSES QNNVAEVGQI VPVQLANSSV YYIPGRQQAS ATGSIFIPKH T FSVYHVQE ELTQEQALNL TKLVNIIEML LESRSKKDFK QICFFEKLYY TYSISSDEIL DLKIWKGPKG KEMSRLKPCN VL SFLYDAL KNKNSSLGFW ARPPNLLKSS PLAYQQDQNS FNATELPIIC SAEVMFVTLL KEIINYLQFI NDLCDTFNNE QLI KRHENI WMLIEQRKIG HDF UniProtKB: D339L |
-Macromolecule #3: M1249L
Macromolecule | Name: M1249L / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 144.604125 KDa |
Sequence | String: MEEVITIAQI VHRGTDILSL NNEEIEALVD EIYSTLKGSN DIKNIRLIDF LFTLKDFVNH VRAEQSKLPD LSMPIEAYIR QLLVDPDVV PIVSEKKKEL RVRPSTRKEI FLINGTHLAV PAEAPIEIYG LKLRLKTFSP QCFMRMAEIG SFSPETLGYV A SGANLTNF ...String: MEEVITIAQI VHRGTDILSL NNEEIEALVD EIYSTLKGSN DIKNIRLIDF LFTLKDFVNH VRAEQSKLPD LSMPIEAYIR QLLVDPDVV PIVSEKKKEL RVRPSTRKEI FLINGTHLAV PAEAPIEIYG LKLRLKTFSP QCFMRMAEIG SFSPETLGYV A SGANLTNF IRVFMKCVDQ ETWKKNGEGV VVTTKENIIQ FTHQYIELYK FLRSGGHSWL INRLAEEMVH RKLDREDQGS HI SNIVETE EIEPEENIKR VIFFLKELST MYSVSPVFTS GYMPLLYDLY RAGYLEVLWN PVEQKFLQHA EQREKEQMIL QQV DMKLTE VITQARQYFK IMEEKIGRVQ SDAIREILTM EGKVDDPNSI LQEVIKACGK QEAELITTEY LNIKKQWELQ EKNA CAHLK LVKQLRSGLQ YAELLKVLES IRVLYKEKNN TTNWNLCKAC GFKLLCPHVD MLIQLQAAEA SYDTMRTKLM KFSGI NKEK ENNQGLIYSY FCKICGEELA HFIQEDRTAD VGIIGDLNSK LRVFIWQETM KACTFIHFGK LVDVKQFANI AVNVCL PLV YSIENIKKEE DYDPLTQLYA VIYIYAYILN LIYSSQKNKE FLTITIHGMK ADSSLNAYVT FLLEKMMQQY SGIINQL SE ITDQWIANNF REAFKKIIHQ NGLQGLSVQD DTKVLLTEIL LDPMYDYAAT VARIDGSIPM HKPRTPKEAE YEFKTVIG R TPAELLSQKE FYDKIYTSKY RPDFTQLTRL NDIYFQEESL RVWWGGRDEE KTSTLIYLRA YELFLKYLQN APNFNSELA EFKTYENAYG EQKALLAQQG FYNIFDPNTG RADQRTRLFE YKRLPISTLY DERGLPHKWT IYVYKAVDSS QKPAEIEVTR KDVIKKIDN HYALADLRCS VCHVLQHEVG QLNIKKVQTA LKASLEFNTF YAFYESRCPK GGLHDFQDKK CVKCGLFTYI I YDHLSQPE LVHDYYNNYK DQYDKEKMSI RSIQIKKDMT TPSTETQPKP PQEPWTFDYG KIIKTAKILD ISPAVIEAIG AM EGRSYAD IREGQGAPPP PTSMDDPRLM AVDSAVRIFL YNYNCLRHVS TFNKPPIHVE RLVKHLSYEE KEDLEKVLPN VVN EYHTTF KHLRVTDPAS ALLYSIEFLC ISFLTLYEIK EPSWVVNIVR EFALTELNTI IQSEKLLSKP GAFNFMIFGE DFVC SGEDS SMDDISAYSS PGLFGEDIID RLDDPFSIED VDISLDVLDN LAPQ UniProtKB: M1249L |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 1.25 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.0 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |