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- PDB-8kdb: Cryo-EM structure of the human parainfluenza virus hPIV3 L-P poly... -
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Open data
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Basic information
Entry | Database: PDB / ID: 8kdb | ||||||
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Title | Cryo-EM structure of the human parainfluenza virus hPIV3 L-P polymerase in dimeric form | ||||||
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![]() | VIRAL PROTEIN / dimeric polymerase / parainfluenza virus / L-P polymerase / cryo-EM structure / non-segmented negative-strand RNA virus / L-L dimerization / RNA replication / RdRp active site | ||||||
Function / homology | ![]() GDP polyribonucleotidyltransferase / Hydrolases; Acting on acid anhydrides; In phosphorus-containing anhydrides / viral genome replication / Transferases; Transferring one-carbon groups; Methyltransferases / virion component / mRNA 5'-cap (guanine-N7-)-methyltransferase activity / host cell cytoplasm / RNA-directed RNA polymerase / RNA-dependent RNA polymerase activity / GTPase activity ...GDP polyribonucleotidyltransferase / Hydrolases; Acting on acid anhydrides; In phosphorus-containing anhydrides / viral genome replication / Transferases; Transferring one-carbon groups; Methyltransferases / virion component / mRNA 5'-cap (guanine-N7-)-methyltransferase activity / host cell cytoplasm / RNA-directed RNA polymerase / RNA-dependent RNA polymerase activity / GTPase activity / DNA-templated transcription / RNA binding / ATP binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.7 Å | ||||||
![]() | Xie, J. / Wang, L. / Zhai, G. / Wu, D. / Lin, Z. / Wang, M. / Yan, X. / Gao, L. / Huang, X. / Fearns, R. / Chen, S. | ||||||
Funding support | 1items
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![]() | ![]() Title: Structural basis for dimerization of a paramyxovirus polymerase complex. Authors: Jin Xie / Mohamed Ouizougun-Oubari / Li Wang / Guanglei Zhai / Daitze Wu / Zhaohu Lin / Manfu Wang / Barbara Ludeke / Xiaodong Yan / Tobias Nilsson / Lu Gao / Xinyi Huang / Rachel Fearns / Shuai Chen / ![]() ![]() ![]() Abstract: The transcription and replication processes of non-segmented, negative-strand RNA viruses (nsNSVs) are catalyzed by a multi-functional polymerase complex composed of the large protein (L) and a ...The transcription and replication processes of non-segmented, negative-strand RNA viruses (nsNSVs) are catalyzed by a multi-functional polymerase complex composed of the large protein (L) and a cofactor protein, such as phosphoprotein (P). Previous studies have shown that the nsNSV polymerase can adopt a dimeric form, however, the structure of the dimer and its function are poorly understood. Here we determine a 2.7 Å cryo-EM structure of human parainfluenza virus type 3 (hPIV3) L-P complex with the connector domain (CD') of a second L built, while reconstruction of the rest of the second L-P obtains a low-resolution map of the ring-like L core region. This study reveals detailed atomic features of nsNSV polymerase active site and distinct conformation of hPIV3 L with a unique β-strand latch. Furthermore, we report the structural basis of L-L dimerization, with CD' located at the putative template entry of the adjoining L. Disruption of the L-L interface causes a defect in RNA replication that can be overcome by complementation, demonstrating that L dimerization is necessary for hPIV3 genome replication. These findings provide further insight into how nsNSV polymerases perform their functions, and suggest a new avenue for rational drug design. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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PDBx/mmCIF format | ![]() | 545 KB | Display | ![]() |
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PDB format | ![]() | 396.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 1.2 MB | Display | ![]() |
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Full document | ![]() | 1.2 MB | Display | |
Data in XML | ![]() | 77.6 KB | Display | |
Data in CIF | ![]() | 117.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 37130MC ![]() 8kdcC M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Components
#1: Protein | Mass: 260103.703 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: NP_067153.2 / Source: (gene. exp.) ![]() ![]() ![]() #2: Protein | Mass: 68471.312 Da / Num. of mol.: 5 Source method: isolated from a genetically manipulated source Details: NP_067149.1 / Source: (gene. exp.) ![]() ![]() ![]() #3: Chemical | ChemComp-MG / | #4: Chemical | Has ligand of interest | Y | |
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-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: Human parainfluenza virus hPIV3 L-P polymerase in dimeric form Type: COMPLEX / Entity ID: #1-#2 / Source: RECOMBINANT |
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Source (natural) | Organism: ![]() |
Source (recombinant) | Organism: ![]() ![]() |
Buffer solution | pH: 7.5 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | 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 / Nominal defocus max: 2000 nm / Nominal defocus min: 1500 nm |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
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Processing
Image processing |
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CTF correction |
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3D reconstruction |
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Refinement | Highest resolution: 2.7 Å |