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- EMDB-60923: Cryo-EM structure of the full-length Nipah Virus L Protein bound ... -

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Entry
Database: EMDB / ID: EMD-60923
TitleCryo-EM structure of the full-length Nipah Virus L Protein bound by Phosphoprotein Tetramer
Map data
Sample
  • Complex: Cryo-EM structure of the full-length Nipah Virus L Protein bound by Phosphoprotein Tetramer
    • Protein or peptide: RNA-directed RNA polymerase L
    • Protein or peptide: Phosphoprotein
  • Ligand: ZINC ION
KeywordsRNA polymerase / VIRAL PROTEIN
Function / homology
Function and homology information


negative stranded viral RNA transcription / NNS virus cap methyltransferase / GDP polyribonucleotidyltransferase / negative stranded viral RNA replication / Hydrolases; Acting on acid anhydrides; In phosphorus-containing anhydrides / virion component / molecular adaptor activity / mRNA 5'-cap (guanine-N7-)-methyltransferase activity / host cell cytoplasm / symbiont-mediated suppression of host innate immune response ...negative stranded viral RNA transcription / NNS virus cap methyltransferase / GDP polyribonucleotidyltransferase / negative stranded viral RNA replication / Hydrolases; Acting on acid anhydrides; In phosphorus-containing anhydrides / virion component / molecular adaptor activity / mRNA 5'-cap (guanine-N7-)-methyltransferase activity / host cell cytoplasm / symbiont-mediated suppression of host innate immune response / RNA-directed RNA polymerase / RNA-directed RNA polymerase activity / GTPase activity / ATP binding
Similarity search - Function
Phosphoprotein P region PNT disordered / Phosphoprotein P region PNT disordered / Paramyxovirus structural protein P/V, N-terminal domain / Paramyxovirus structural protein V/P N-terminus / Phosphoprotein P soyouz module / N-terminal region of Paramyxovirinae phosphoprotein (P) / RNA-directed RNA polymerase, paramyxovirus / P/V phosphoprotein, paramyxoviral / Paramyxovirus P/V phosphoprotein C-terminal / Mononegavirales RNA-directed RNA polymerase catalytic domain ...Phosphoprotein P region PNT disordered / Phosphoprotein P region PNT disordered / Paramyxovirus structural protein P/V, N-terminal domain / Paramyxovirus structural protein V/P N-terminus / Phosphoprotein P soyouz module / N-terminal region of Paramyxovirinae phosphoprotein (P) / RNA-directed RNA polymerase, paramyxovirus / P/V phosphoprotein, paramyxoviral / Paramyxovirus P/V phosphoprotein C-terminal / Mononegavirales RNA-directed RNA polymerase catalytic domain / Mononegavirus L protein 2-O-ribose methyltransferase / Mononegavirales mRNA-capping domain V / RNA-directed RNA polymerase L, C-terminal / Mononegavirales RNA dependent RNA polymerase / Mononegavirales mRNA-capping region V / RdRp of negative ssRNA viruses with non-segmented genomes catalytic domain profile. / Mononegavirus L protein 2'-O-ribose methyltransferase domain profile. / Ribosomal RNA methyltransferase, FtsJ domain / FtsJ-like methyltransferase
Similarity search - Domain/homology
RNA-directed RNA polymerase L / Phosphoprotein
Similarity search - Component
Biological speciesHenipavirus nipahense
Methodsingle particle reconstruction / cryo EM / Resolution: 2.52 Å
AuthorsXue L / Chang T / Gui J / Li Z / Zhao H / Zou B / Li M / He J / Chen X / Xiong X
Funding support China, 1 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)82341085 to X.X. China
CitationJournal: Protein Cell / Year: 2025
Title: Cryo-EM structures of Nipah virus polymerase complex reveal highly varied interactions between L and P proteins among paramyxoviruses.
Authors: Lu Xue / Tiancai Chang / Jiacheng Gui / Zimu Li / Heyu Zhao / Bingqian Zou / Junnan Lu / Mei Li / Xin Wen / Shenghua Gao / Peng Zhan / Lijun Rong / Liqiang Feng / Peng Gong / Jun He / Xinwen ...Authors: Lu Xue / Tiancai Chang / Jiacheng Gui / Zimu Li / Heyu Zhao / Bingqian Zou / Junnan Lu / Mei Li / Xin Wen / Shenghua Gao / Peng Zhan / Lijun Rong / Liqiang Feng / Peng Gong / Jun He / Xinwen Chen / Xiaoli Xiong /
Abstract: Nipah virus (NiV) and related viruses form a distinct henipavirus genus within the Paramyxoviridae family. NiV continues to spillover into the humans causing deadly outbreaks with increasing human- ...Nipah virus (NiV) and related viruses form a distinct henipavirus genus within the Paramyxoviridae family. NiV continues to spillover into the humans causing deadly outbreaks with increasing human-bat interaction. NiV encodes the large protein (L) and phosphoprotein (P) to form the viral RNA polymerase machinery. Their sequences show limited homologies to those of non-henipavirus paramyxoviruses. We report two cryo-electron microscopy (cryo-EM) structures of the Nipah virus (NiV) polymerase L-P complex, expressed and purified in either its full-length or truncated form. The structures resolve the RNA-dependent RNA polymerase (RdRp) and polyribonucleotidyl transferase (PRNTase) domains of the L protein, as well as a tetrameric P protein bundle bound to the L-RdRp. L-protein C-terminal regions are unresolved, indicating flexibility. Two PRNTase domain zinc-binding sites, conserved in most Mononegavirales, are confirmed essential for NiV polymerase activity. The structures further reveal anchoring of the P protein bundle and P protein X domain (XD) linkers on L, via an interaction pattern distinct among Paramyxoviridae. These interactions facilitate binding of a P protein XD linker in the nucleotide entry channel and distinct positioning of other XD linkers. We show that the disruption of the L-P interactions reduces NiV polymerase activity. The reported structures should facilitate rational antiviral-drug discovery and provide a guide for the functional study of NiV polymerase.
History
DepositionJul 23, 2024-
Header (metadata) releaseMay 21, 2025-
Map releaseMay 21, 2025-
UpdateMay 21, 2025-
Current statusMay 21, 2025Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_60923.png

Downloads & links

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Map

FileDownload / File: emd_60923.map.gz / Format: CCP4 / Size: 91.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

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AxesZ (Sec.)Y (Row.)X (Col.)
0.91 Å/pix.
x 288 pix.
= 262.8 Å		0.91 Å/pix.
x 288 pix.
= 262.8 Å		0.91 Å/pix.
x 288 pix.
= 262.8 Å

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Images are generated by Spider.

Voxel sizeX=Y=Z: 0.9125 Å
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Histogram (log scale)
Contour LevelBy AUTHOR: 0.13
Minimum - Maximum-1.0524101 - 2.0716996
Average (Standard dev.)0.00064248126 (±0.051509596)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions288288288
Spacing288288288
CellA=B=C: 262.80002 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_60923_msk_1.map
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Half map: #2

Fileemd_60923_half_map_1.map
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Half map: #1

Fileemd_60923_half_map_2.map
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Sample components

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Entire : Cryo-EM structure of the full-length Nipah Virus L Protein bound ...

EntireName: Cryo-EM structure of the full-length Nipah Virus L Protein bound by Phosphoprotein Tetramer
Components
  • Complex: Cryo-EM structure of the full-length Nipah Virus L Protein bound by Phosphoprotein Tetramer
    • Protein or peptide: RNA-directed RNA polymerase L
    • Protein or peptide: Phosphoprotein
  • Ligand: ZINC ION

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Supramolecule #1: Cryo-EM structure of the full-length Nipah Virus L Protein bound ...

SupramoleculeName: Cryo-EM structure of the full-length Nipah Virus L Protein bound by Phosphoprotein Tetramer
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2
Source (natural)Organism: Henipavirus nipahense

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Macromolecule #1: RNA-directed RNA polymerase L

MacromoleculeName: RNA-directed RNA polymerase L / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: RNA-directed RNA polymerase
Source (natural)Organism: Henipavirus nipahense
Molecular weightTheoretical: 257.565156 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MADELSISDI IYPECHLDSP IVSGKLISAI EYAQLRHNQP SDDKRLSENI RLNLHGKRKS LYILRQSKQG DYIRNNIKNL KEFMHIAYP ECNNILFSIT SQGMTSKLDN IMKKSFKAYN IISKKVIGML QNITRNLITQ DRRDEIINIH ECRRLGDLGK N MSQSKWYE ...String:
MADELSISDI IYPECHLDSP IVSGKLISAI EYAQLRHNQP SDDKRLSENI RLNLHGKRKS LYILRQSKQG DYIRNNIKNL KEFMHIAYP ECNNILFSIT SQGMTSKLDN IMKKSFKAYN IISKKVIGML QNITRNLITQ DRRDEIINIH ECRRLGDLGK N MSQSKWYE CFLFWFTIKT EMRAVIKNSQ KPKFRSDSCI IHMRDKSTEI ILNPNLICIF KSDKTGKKCY YLTPEMVLMY CD VLEGRMM METTVKSDIK YQPLISRSNA LWGLIDPLFP VMGNRIYNIV SMIEPLVLAL LQLKDEARIL RGAFLHHCIK EMH QELSEC GFTDQKIRSM FIDDLLSILN IDNIHLLAEF FSFFRTFGHP ILEAKVAAEK VREHMLADKV LEYAPIMKAH AIFC GTIIN GYRDRHGGAW PPLYLPAHAS KHIIRLKNSG ESLTIDDCVK NWESFCGIQF DCFMELKLDS DLSMYMKDKA LSPIK DEWD SVYPREVLSY TPPKSTEPRR LVDVFVNDEN FDPYNMLEYV LSGAYLEDEQ FNVSYSLKEK ETKQAGRLFA KMTYKM RAC QVIAEALIAS GVGKYFKENG MVKDEHELLK TLFQLSISSV PRGNSQGNDP QSINNIERDF QYFKGVTTNV KDKKNNS FN KVKSALNNPC QADGVHHNMS PNTRNRYKCS NTSKSFLDYH TEFNPHNHYK SDNTEAAVLS RYEDNTGTKF DTVSAFLT T DLKKFCLNWR YESMAIFAER LDEIYGLPGF FNWMHKRLER SVIYVADPNC PPNIDKHMEL EKTPEDDIFI HYPKGGIEG YSQKTWTIAT IPFLFLSAYE TNTRIAAIVQ GDNESIAITQ KVHPNLPYKV KKEICAKQAQ LYFERLRMNL RALGHNLKAT ETIISTHLF IYSKKIHYDG AVLSQALKSM SRCCFWSETL VDETRSACSN ISTTIAKAIE NGLSRNVGYC INILKVIQQL L ISTEFSIN ETLTLDVTSP ISNNLDWLIT AALIPAPIGG FNYLNLSRIF VRNIGDPVTA SLADLKRMID HSIMTESVLQ KV MNQEPGD ASFLDWASDP YSGNLPDSQS ITKTIKNITA RTILRNSPNP MLKGLFHDKS FDEDLELASF LMDRRVILPR AAH EILDNS LTGAREEIAG LLDTTKGLIR SGLRKSGLQP KLVSRLSHHD YNQFLILNKL LSNRRQNDLI SSNTCSVDLA RALR SHMWR ELALGRVIYG LEVPDALEAM VGRYITGSLE CQICEQGNTM YGWFFVPRDS QLDQVDREHS SIRVPYVGSS TDERS DIKL GNVKRPTKAL RSAIRIATVY TWAYGDNEEC WYEAWYLASQ RVNIDLDVLK AITPVSTSNN LSHRLRDKST QFKFAG SVL NRVSRYVNIS NDNLDFRIEG EKVDTNLIYQ QAMLLGLSVL EGKFRLRLET DDYNGIYHLH VKDNCCVKEV ADVGQVD AE LPIPEYTEVD NNHLIYDPDP VSEIDCSRLS NQESKSRELD FPLWSTEELH DVLAKTVAQT VLEIITKADK DVLKQHLA I DSDDNINSLI TEFLIVDPEL FALYLGQSIS IKWAFEIHHR RPRGRHTMVD LLSDLVSNTS KHTYKVLSNA LSHPRVFKR FVNCGLLLPT QGPYLHQQDF EKLSQNLLVT SYMIYLMNWC DFKKSPFLIA EQDETVISLR EDIITSKHLC VIIDLYANHH KPPWIIDLN PQEKICVLRD FISKSRHVDT SSRSWNTSDL DFVIFYASLT YLRRGIIKQL RIRQVTEVID TTTMLRDNII V ENPPIKTG VLDIRGCIIY NLEEILSMNT KSASKKIFNL NSRPSVENHK YRRIGLNSSS CYKALNLSPL IQRYLPSGAQ RL FIGEGSG SMMLLYQSTL GQSISFYNSG IDGDYIPGQR ELKLFPSEYS IAEEDPSLTG KLKGLVVPLF NGRPETTWIG NLD SYEYII NRTAGRSIGL VHSDMESGID KNVEEILVEH SHLISIAINV MMEDGLLVSK IAYTPGFPIS RLFNMYRSYF GLVL VCFPV YSNPDSTEVY LLCLQKTVKT IVPPQKVLEH SNLHDEVNDQ GITSVIFKIK NSQSKQFHDD LKKYYQIDQP FFVPT KITS DEQVLLQAGL KLNGPEILKS EISYDIGSDI NTLRDTIIIM LNEAMNYFDD NRSPSHHLEP YPVLERTRIK TIMNCV TKK VIVYSLIKFK DTKSSELYHI KNNIRRKVLI LDFRSKLMTK TLPKGMQERR EKNGFKEVWI VDLSNREVKI WWKIIGY IS II

UniProtKB: RNA-directed RNA polymerase L

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Macromolecule #2: Phosphoprotein

MacromoleculeName: Phosphoprotein / type: protein_or_peptide / ID: 2 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Henipavirus nipahense
Molecular weightTheoretical: 78.39032 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MDKLELVNDG LNIIDFIQKN QKEIQKTYGR SSIQQPSIKD QTKAWEDFLQ CTSGESEQVE GGMSKDDGDV ERRNLEDLSS TSPTDGTIG KRVSNTRDWA EGSDDIQLDP VVTDVVYHDH GGECTGYGFT SSPERGWSDY TSGANNGNVC LVSDAKMLSY A PEIAVSKE ...String:
MDKLELVNDG LNIIDFIQKN QKEIQKTYGR SSIQQPSIKD QTKAWEDFLQ CTSGESEQVE GGMSKDDGDV ERRNLEDLSS TSPTDGTIG KRVSNTRDWA EGSDDIQLDP VVTDVVYHDH GGECTGYGFT SSPERGWSDY TSGANNGNVC LVSDAKMLSY A PEIAVSKE DRETDLVHLE NKLSTTGLNP TAVPFTLRNL SDPAKDSPVI AEHYYGLGVK EQNVGPQTSR NVNLDSIKLY TS DDEEADQ LEFEDEFAGS SSEVIVGISP EDEEPSSVGG KPNESIGRTI EGQSIRDNLQ AKDNKSTDVP GAGPKDSAVK EEP PQKRLP MLAEEFECSG SEDPIIRELL KENSLINCQQ GKDAQPPYHW SIERSISPDK TEIVNGAVQT ADRQRPGTPM PKSR GIPIK KGTDAKYPSA GTENVPGSKS GATRHVRGSP PYQEGKSVNA ENVQLNASTA VKETDKSEVN PVDDNDSLDD KYIMP SDDF SNTFFPHDTD RLNYHADHLG DYDLETLCEE SVLMGVINSI KLINLDMRLN HIEEQVKEIP KIINKLESID RVLAKT NTA LSTIEGHLVS MMIMIPGKGK GERKGKNNPE LKPVIGRDIL EQQSLFSFDN VKNFRDGSLT NEPYGAAVQL REDLILP EL NFEETNASQF VPMADDSSRD VIKTLIRTHI KDRELRSELI GYLNKAENDE EIQEIANTVN DIIDGNI

UniProtKB: Phosphoprotein

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Macromolecule #3: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 3 / Number of copies: 2 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 8
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: TFS FALCON 4i (4k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.4 µm / Nominal defocus min: 0.6 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.52 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 224424
Initial angle assignmentType: PROJECTION MATCHING
Final angle assignmentType: PROJECTION MATCHING
FSC plot (resolution estimation)

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