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- PDB-6pzk: Cryo-EM Structure of the Respiratory Syncytial Virus Polymerase (... -
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Basic information
Entry | Database: PDB / ID: 6pzk | ||||||
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Title | Cryo-EM Structure of the Respiratory Syncytial Virus Polymerase (L) Protein Bound by the Tetrameric Phosphoprotein (P) | ||||||
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![]() | VIRAL PROTEIN / RNA-binding protein / RSV / RdRp / RNA-dependent RNA polymerase / PRNTase / polyribonucleotidyl transferase / RNA capping / viral replication | ||||||
Function / homology | ![]() NNS virus cap methyltransferase / GDP polyribonucleotidyltransferase / Respiratory syncytial virus genome transcription / Translation of respiratory syncytial virus mRNAs / negative stranded viral RNA replication / Respiratory syncytial virus genome replication / RSV-host interactions / Maturation of hRSV A proteins / Assembly and release of respiratory syncytial virus (RSV) virions / Respiratory syncytial virus (RSV) attachment and entry ...NNS virus cap methyltransferase / GDP polyribonucleotidyltransferase / Respiratory syncytial virus genome transcription / Translation of respiratory syncytial virus mRNAs / negative stranded viral RNA replication / Respiratory syncytial virus genome replication / RSV-host interactions / Maturation of hRSV A proteins / Assembly and release of respiratory syncytial virus (RSV) virions / Respiratory syncytial virus (RSV) attachment and entry / Hydrolases; Acting on acid anhydrides; In phosphorus-containing anhydrides / viral life cycle / virion component / mRNA 5'-cap (guanine-N7-)-methyltransferase activity / host cell cytoplasm / RNA-directed RNA polymerase / RNA-dependent RNA polymerase activity / GTPase activity / ATP binding / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.2 Å | ||||||
![]() | Gilman, M.S.A. / McLellan, J.S. | ||||||
![]() | ![]() Title: Structure of the Respiratory Syncytial Virus Polymerase Complex. Authors: Morgan S A Gilman / Cheng Liu / Amy Fung / Ishani Behera / Paul Jordan / Peter Rigaux / Nina Ysebaert / Sergey Tcherniuk / Julien Sourimant / Jean-François Eléouët / Priscila Sutto-Ortiz ...Authors: Morgan S A Gilman / Cheng Liu / Amy Fung / Ishani Behera / Paul Jordan / Peter Rigaux / Nina Ysebaert / Sergey Tcherniuk / Julien Sourimant / Jean-François Eléouët / Priscila Sutto-Ortiz / Etienne Decroly / Dirk Roymans / Zhinan Jin / Jason S McLellan / ![]() ![]() ![]() Abstract: Numerous interventions are in clinical development for respiratory syncytial virus (RSV) infection, including small molecules that target viral transcription and replication. These processes are ...Numerous interventions are in clinical development for respiratory syncytial virus (RSV) infection, including small molecules that target viral transcription and replication. These processes are catalyzed by a complex comprising the RNA-dependent RNA polymerase (L) and the tetrameric phosphoprotein (P). RSV P recruits multiple proteins to the polymerase complex and, with the exception of its oligomerization domain, is thought to be intrinsically disordered. Despite their critical roles in RSV transcription and replication, structures of L and P have remained elusive. Here, we describe the 3.2-Å cryo-EM structure of RSV L bound to tetrameric P. The structure reveals a striking tentacular arrangement of P, with each of the four monomers adopting a distinct conformation. The structure also rationalizes inhibitor escape mutants and mutations observed in live-attenuated vaccine candidates. These results provide a framework for determining the molecular underpinnings of RSV replication and transcription and should facilitate the design of effective RSV inhibitors. | ||||||
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Structure visualization
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Structure viewer | Molecule: ![]() ![]() |
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PDBx/mmCIF format | ![]() | 328.3 KB | Display | ![]() |
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PDB format | ![]() | 244.7 KB | Display | ![]() |
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-Validation report
Summary document | ![]() | 923.2 KB | Display | ![]() |
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Full document | ![]() | 933.9 KB | Display | |
Data in XML | ![]() | 48 KB | Display | |
Data in CIF | ![]() | 74.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 20536MC M: map data used to model this data C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Components
#1: Protein | Mass: 254482.750 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P28887, RNA-directed RNA polymerase, mRNA (guanine-N7)-methyltransferase, Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases, GDP polyribonucleotidyltransferase |
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#2: Protein | Mass: 29062.895 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
Component | Name: Respiratory Syncytial Virus Polymerase (L) Protein Bound by the Tetrameric Phosphoprotein (P) Type: COMPLEX / Entity ID: all / Source: RECOMBINANT | |||||||||||||||||||||||||
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Molecular weight | Value: 0.37 MDa / Experimental value: NO | |||||||||||||||||||||||||
Source (natural) | Organism: ![]() | |||||||||||||||||||||||||
Source (recombinant) | Organism: ![]() ![]() | |||||||||||||||||||||||||
Buffer solution | pH: 8 | |||||||||||||||||||||||||
Buffer component |
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Specimen | Conc.: 0.29 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | |||||||||||||||||||||||||
Specimen support | Grid material: GOLD | |||||||||||||||||||||||||
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD |
Image recording | Electron dose: 48 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
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Processing
EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | |||||||||||||||
Symmetry | Point symmetry: C1 (asymmetric) | |||||||||||||||
3D reconstruction | Resolution: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 196720 / Symmetry type: POINT |