|Entry||Database: EMDB / ID: EMD-1133|
|Title||The structure of the poliovirus 135S cell entry intermediate at 10-angstrom resolution reveals the location of an externalized polypeptide that binds to membranes.|
|Sample||Poliovirus 135S particle:|
|Function / homology|
Function and homology information
suppression by virus of host translation initiation factor activity / suppression by virus of host MDA-5 activity / suppression by virus of host RIG-I activity / picornain 2A / pore-mediated entry of viral genome into host cell / suppression by virus of host mRNA export from nucleus / picornain 3C / suppression by virus of host MAVS activity / T=pseudo3 icosahedral viral capsid / host cell cytoplasmic vesicle membrane ...suppression by virus of host translation initiation factor activity / suppression by virus of host MDA-5 activity / suppression by virus of host RIG-I activity / picornain 2A / pore-mediated entry of viral genome into host cell / suppression by virus of host mRNA export from nucleus / picornain 3C / suppression by virus of host MAVS activity / T=pseudo3 icosahedral viral capsid / host cell cytoplasmic vesicle membrane / RNA-protein covalent cross-linking / positive stranded viral RNA replication / integral to membrane of host cell / pore formation by virus in membrane of host cell / virion assembly / viral capsid / protein complex oligomerization / endocytosis involved in viral entry into host cell / nucleoside-triphosphate phosphatase / ion channel activity / induction by virus of host autophagy / RNA-directed RNA polymerase / cysteine-type endopeptidase activity / viral RNA genome replication / RNA-directed 5'-3' RNA polymerase activity / RNA helicase activity / transcription, DNA-templated / virion attachment to host cell / host cell nucleus / structural molecule activity / RNA binding / membrane / ATP binding / metal ion binding
Viral coat protein subunit / Picornavirus coat protein VP4 / Poliovirus core protein 3a, soluble domain / Peptidase C3, picornavirus core protein 2A / Picornavirus/Calicivirus coat protein / Peptidase C3A/C3B, picornaviral / Helicase, superfamily 3, single-stranded DNA/RNA virus / RNA-directed RNA polymerase, C-terminal domain / Picornavirus capsid / Reverse transcriptase/Diguanylate cyclase domain ...Viral coat protein subunit / Picornavirus coat protein VP4 / Poliovirus core protein 3a, soluble domain / Peptidase C3, picornavirus core protein 2A / Picornavirus/Calicivirus coat protein / Peptidase C3A/C3B, picornaviral / Helicase, superfamily 3, single-stranded DNA/RNA virus / RNA-directed RNA polymerase, C-terminal domain / Picornavirus capsid / Reverse transcriptase/Diguanylate cyclase domain / Picornavirus 2B protein / DNA/RNA polymerase superfamily / RNA-directed RNA polymerase, catalytic domain / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan / Helicase, superfamily 3, single-stranded RNA virus / Poliovirus 3A protein-like / Picornavirales 3C/3C-like protease domain / P-loop containing nucleoside triphosphate hydrolase
|Biological species||Human poliovirus 1 Mahoney (poliovirus)|
|Method||single particle reconstruction / cryo EM / Resolution: 9.6 Å|
|Authors||Bubeck D / Filman DJ / Cheng N / Steven AC / Hogle JM / Belnap DM|
|Citation||Journal: J Virol / Year: 2005|
Title: The structure of the poliovirus 135S cell entry intermediate at 10-angstrom resolution reveals the location of an externalized polypeptide that binds to membranes.
Authors: Doryen Bubeck / David J Filman / Naiqian Cheng / Alasdair C Steven / James M Hogle / David M Belnap /
Abstract: Poliovirus provides a well-characterized system for understanding how nonenveloped viruses enter and infect cells. Upon binding its receptor, poliovirus undergoes an irreversible conformational ...Poliovirus provides a well-characterized system for understanding how nonenveloped viruses enter and infect cells. Upon binding its receptor, poliovirus undergoes an irreversible conformational change to the 135S cell entry intermediate. This transition involves shifts of the capsid protein beta barrels, accompanied by the externalization of VP4 and the N terminus of VP1. Both polypeptides associate with membranes and are postulated to facilitate entry by forming a translocation pore for the viral RNA. We have calculated cryo-electron microscopic reconstructions of 135S particles that permit accurate placement of the beta barrels, loops, and terminal extensions of the capsid proteins. The reconstructions and resulting models indicate that each N terminus of VP1 exits the capsid though an opening in the interface between VP1 and VP3 at the base of the canyon that surrounds the fivefold axis. Comparison with reconstructions of 135S particles in which the first 31 residues of VP1 were proteolytically removed revealed that the externalized N terminus is located near the tips of propeller-like features surrounding the threefold axes rather than at the fivefold axes, as had been proposed in previous models. These observations have forced a reexamination of current models for the role of the 135S particle in transmembrane pore formation and suggest testable alternatives.
|Validation Report||Summary, Full report, XML, About validation report|
|Structure viewer||EM map: |
Downloads & links
|File||Download / File: emd_1133.map.gz / Format: CCP4 / Size: 28.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 1.816 Å|
|Symmetry||Space group: 1|
CCP4 map header:
-Entire Poliovirus 135S particle
|Entire||Name: Poliovirus 135S particle|
Details: Sedimentation coefficient = 135S. Poliovirus 135S particle produced by heating 160S particles at 50 deg. C for 3 minutes.
Oligomeric State: icosahedrally ordered capsid, 60 copies of VP1, VP2, VP3
Number of components: 1
-Component #1: virus, Human poliovirus 1 Mahoney
|Virus||Name: Human poliovirus 1 Mahoney / a.k.a: poliovirus / Class: VIRION / Details: 135S particle / Empty: No / Enveloped: No / Isolate: STRAIN|
|Species||Species: Human poliovirus 1 Mahoney (poliovirus)|
|Source (natural)||Host Species: Homo sapiens (human) / Host category: VERTEBRATES|
|Shell #1||Name of element: capsid / Diameter: 339 Å / T number (triangulation number): 1|
|Specimen||Specimen state: Particle / Method: cryo EM|
|Sample solution||Buffer solution: 20 mM Tris, 2 mM CaCl2 / pH: 7.5|
|Vitrification||Cryogen name: ETHANE / Method: Blotted manually before plunging|
Details: Vitrification carried out in ambient atmosphere. Ethane cooled by liquid nitrogen.
-Electron microscopy imaging
|Imaging||Microscope: FEI/PHILIPS CM200FEG|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 120 kV / Electron dose: 10 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Magnification: 38000 X (nominal), 38500 X (calibrated) / Cs: 2 mm / Imaging mode: BRIGHT FIELD|
|Specimen Holder||Holder: Side entry liquid nitrogen-cooled cryo specimen holder|
Model: GATAN LIQUID NITROGEN
|Camera||Detector: KODAK SO-163 FILM|
|Image acquisition||Number of digital images: 6 / Scanner: ZEISS SCAI / Sampling size: 7 µm / Bit depth: 8 |
Details: Defocal pairs were used. Here, corresponding particle images from each micrograph are counted as one. Three focal pairs were scanned.
|Processing||Method: single particle reconstruction / Number of projections: 8224 |
Details: Poliovirus 135S particle produced by heating 160S particles at 50 deg. C for 3 minutes.
Applied symmetry: I (icosahedral)
|3D reconstruction||Algorithm: Fourier Bessel / Software: EM3DR2 / CTF correction: CTF and decay correction of each particle / Resolution: 9.6 Å / Resolution method: FSC 0.333|
Euler angles: Determined via PFT2 using both amplitude and phase information to determine best view. Focal pairs summed for orientation determination only.
Details: Reconstructed computed from focal pairs. Pairs not summed for reconstruction calculaton.
-Atomic model buiding
|Modeling #1||Refinement protocol: rigid body / Refinement space: RECIPROCAL|
Details: Protocol: rigid body. see paper for details of the model fitting
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