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Yorodumi- EMDB-66473: Cryo-EM structure of Borna disease virus RNA polymerase L protein -
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Open data
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Basic information
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| Title | Cryo-EM structure of Borna disease virus RNA polymerase L protein | |||||||||
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Sample |
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Keywords | Polymerase / Viral protein | |||||||||
| Function / homology | Function and homology informationvirion component / mRNA 5'-cap (guanine-N7-)-methyltransferase activity / RNA-directed RNA polymerase / RNA-directed RNA polymerase activity / host cell nucleus / ATP binding Similarity search - Function | |||||||||
| Biological species | Borna disease virus-V | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.83 Å | |||||||||
Authors | Ma J / Yang K / Wu H / Liang Z | |||||||||
| Funding support | 1 items
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Citation | Journal: Cell Rep / Year: 2026Title: Structural mechanism of Borna disease virus 1 RNA polymerase autoinhibition and suramin-mediated inhibition. Authors: Kankan Yang / Haiqiang Wu / Zuxing Liang / Junwei Zou / Jun Ma / ![]() Abstract: Borna disease virus 1 (BoDV-1) is a neurotropic pathogen that causes severe, often fatal encephalitis, yet effective treatments remain unavailable. As a nuclear-replicating mononegavirus, BoDV-1 ...Borna disease virus 1 (BoDV-1) is a neurotropic pathogen that causes severe, often fatal encephalitis, yet effective treatments remain unavailable. As a nuclear-replicating mononegavirus, BoDV-1 employs a minimal L-P polymerase complex. Here, we report cryo-electron microscopy (cryo-EM) structures of the BoDV-1 polymerase in L-alone, apo-L-P, and inhibitor-bound L-P states, revealing the most compact L protein characterized among mononegaviruses. While the catalytic core is conserved, the C-terminal domains are degenerate, with the methyltransferase-like (MTase-like) domain lacking canonical functional motifs. We identify an N-terminal autoinhibitory element (AIE) that is positioned to physically block the template entry tunnel, suggesting an autoinhibition mechanism reminiscent of a "molecular plug." Furthermore, we demonstrate that the inhibitor suramin binds in a specific triple-molecule mode, potentially achieving inhibition by sterically occluding RNA access and allosterically restricting the catalytic core. These findings elucidate the architecture and regulation of the BoDV-1 polymerase, providing a structural framework for rational antiviral design. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_66473.map.gz | 62.4 MB | EMDB map data format | |
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| Header (meta data) | emd-66473-v30.xml emd-66473.xml | 19.3 KB 19.3 KB | Display Display | EMDB header |
| Images | emd_66473.png | 155.1 KB | ||
| Filedesc metadata | emd-66473.cif.gz | 6.6 KB | ||
| Others | emd_66473_additional_1.map.gz emd_66473_half_map_1.map.gz emd_66473_half_map_2.map.gz | 117.8 MB 115.9 MB 115.9 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-66473 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-66473 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9x28MC ![]() 9x1vC ![]() 9x5rC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_66473.map.gz / Format: CCP4 / Size: 125 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.73 Å | ||||||||||||||||||||||||||||||||||||
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Additional map: #1
| File | emd_66473_additional_1.map | ||||||||||||
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-Half map: #2
| File | emd_66473_half_map_1.map | ||||||||||||
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-Half map: #1
| File | emd_66473_half_map_2.map | ||||||||||||
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Sample components
-Entire : Borna disease virus RNA polymerase complex
| Entire | Name: Borna disease virus RNA polymerase complex |
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| Components |
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-Supramolecule #1: Borna disease virus RNA polymerase complex
| Supramolecule | Name: Borna disease virus RNA polymerase complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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| Source (natural) | Organism: Borna disease virus-V |
| Molecular weight | Theoretical: 192 KDa |
-Macromolecule #1: RNA-directed RNA polymerase L
| Macromolecule | Name: RNA-directed RNA polymerase L / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: RNA-directed RNA polymerase |
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| Source (natural) | Organism: Borna disease virus-V |
| Molecular weight | Theoretical: 194.970875 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MSFHASLLRE EETPRPVAGI NRTDQSLKNP LLGTEVSFCL KSSSLPHHVR ALGQIKARNL ASCDYYLLFR QVVLPPEVYP IGVLIRAAE AILTVIVSAW KLDHMTKTLY SSVRYALTNP RVRAQLELHI AYQRIVGQVS YSREADIGPK RLGNMSLQFI Q SLVIATID ...String: MSFHASLLRE EETPRPVAGI NRTDQSLKNP LLGTEVSFCL KSSSLPHHVR ALGQIKARNL ASCDYYLLFR QVVLPPEVYP IGVLIRAAE AILTVIVSAW KLDHMTKTLY SSVRYALTNP RVRAQLELHI AYQRIVGQVS YSREADIGPK RLGNMSLQFI Q SLVIATID TTSCLMTYNH FLAAADTAKS RCHLLIASVV QGALWEQGSF LDHIINMIDI IDSINLPHDD YFTIIKSIFP YS QGLVMGR HNVSVSSDFA SVFAIPELCP QLDSLLKKLL QLDPVLLLMV SSVQKSWYFP EIRMVDGSRE QLHKMRVELE TPQ ALLSYG HTLLSIFRAE FIKGYVSKNA KWPPVHLLPG CDKSIKNARE LGRWSPAFDR RWQLFEKVVI LRIADLDMDP DFND IVSDK AIISSRRDWV FEYNAAAFWK KYGERLERPP ARSGPSRLVN ALIDGRLDNI PALLEPFYRG AVEFEDRLTV LVPKE KELK VKGRFFSKQT LAIRIYQVVA EAALKNEVMP YLKTHSMTMS STALTHLLNR LSHTITKGDS FVINLDYSSW CNGFRP ELQ APICRQLDQM FNCGYFFRTG CTLPCFTTFI IQDRFNPPYS LSGEPVEDGV TCAVGTKTMG EGMRQKLWTI LTSCWEI IA LREINVTFNI LGQGDNQTII IHKSASQNNQ LLAERALGAL YKHARLAGHN LKVEECWVSD CLYEYGKKLF FRGVPVPG C LKQLSRVTDS TGELFPNLYS KLACLTSSCL SAAMADTSPW VALATGVCLY LIELYVELPP AIIQDESLLT TLCLVGPSI GGLPTPATLP SVFFRGMSDP LPFQLALLQT LIKTTGVTCS LVNRVVKLRI APYPDWLSLV TDPTSLNIAQ VYRPERQIRR WIEEAIATS SHSSRIATFF QQPLTEMAQL LARDLSTMMP LRPRDMSALF ALSNVAYGLS IIDLFQKSST VVSASQAVHI E DVALESVR YKESIIQGLL DTTEGYNMQP YLEGCTYLAA KQLRRLTWGR DLVGVTMPFV AEQFHPHSSV GAKAELYLDA II YCPQETL RSHHLTTRGD QPLYLGSNTA VKVQRGEITG LAKSRAANLV KDTLVLHQWY KVRKVTDPHL NTLMARFLLE KGY TSDARP SIQGGTLTHR LPSRGDSRQG LTGYVNILST WLRFSSDYLH SFSKSSDDYT IHFQHVFTYG CLYADSVIRS GGVI STPYL LSASCKTCFE KIDSEEFVLA CEPQYRGAEW LISKPVTVPE QITDAEVEFD PCVSASYCLG ILIGKSFLVD IRASG HDIM EQRTWANLER FSVSDMQKLP WSIVIRSLWR FLIGARLLQF EKAGLIRMLY AATGPTFSFL MKVFQDSALL MDCAPL DRL SPRINFHSRG DLVAKLVLLP FINPGIVEIE VSGINSKYHA VSEANMDLYI AAAKSVGVKP TQFVEETNDF TARGHHH GC YSLSWSKSRN QSQVLKMVVR KLKLCVLYIY PTVDPAVALD LCHLPALTII LVLGGDPAYY ERLLEMDLCG AVSSRVDI P HSLAARTHRG FAVGPDAGPG VIRLDRLESV CYAHPCLEEL EFNAYLDSEL VDISDMCCLP LATPCKALFR PIYRSLQSF RLALMDNYSF VMDLIMIRGL DIRPHLEEFD ELLVVGQHIL GQPVLVEVVY YVGVVRKRPV LARHPWSADL KRITVGGRAP CPSAARLRD EDCQGSLLVG LPAGLTQLLI IDWSHPQFEK GSSGGSSGSS GGAWSHPQFE K UniProtKB: RNA-directed RNA polymerase L |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 8 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: FEI FALCON IV (4k 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 / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.2 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
| Initial model | Chain - Source name: AlphaFold / Chain - Initial model type: in silico model |
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| Refinement | Protocol: RIGID BODY FIT |
| Output model | ![]() PDB-9x28: |
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Keywords
Borna disease virus-V
Authors
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FIELD EMISSION GUN
