[English] 日本語
Yorodumi Papers
- Database of articles cited by EMDB/PDB/SASBDB data -

+
Search query

Keywords
Structure methods
Author
Journal
IF

-
Structure paper

TitleThe Hantavirus Surface Glycoprotein Lattice and Its Fusion Control Mechanism.
Journal, issue, pagesCell, Vol. 183, Issue 2, Page 442-456.e16, Year 2020
Publish dateOct 15, 2020
AuthorsAlexandra Serris / Robert Stass / Eduardo A Bignon / Nicolás A Muena / Jean-Claude Manuguerra / Rohit K Jangra / Sai Li / Kartik Chandran / Nicole D Tischler / Juha T Huiskonen / Felix A Rey / Pablo Guardado-Calvo /
PubMed AbstractHantaviruses are rodent-borne viruses causing serious zoonotic outbreaks worldwide for which no treatment is available. Hantavirus particles are pleomorphic and display a characteristic square ...Hantaviruses are rodent-borne viruses causing serious zoonotic outbreaks worldwide for which no treatment is available. Hantavirus particles are pleomorphic and display a characteristic square surface lattice. The envelope glycoproteins Gn and Gc form heterodimers that further assemble into tetrameric spikes, the lattice building blocks. The glycoproteins, which are the sole targets of neutralizing antibodies, drive virus entry via receptor-mediated endocytosis and endosomal membrane fusion. Here we describe the high-resolution X-ray structures of the heterodimer of Gc and the Gn head and of the homotetrameric Gn base. Docking them into an 11.4-Å-resolution cryoelectron tomography map of the hantavirus surface accounted for the complete extramembrane portion of the viral glycoprotein shell and allowed a detailed description of the surface organization of these pleomorphic virions. Our results, which further revealed a built-in mechanism controlling Gc membrane insertion for fusion, pave the way for immunogen design to protect against pathogenic hantaviruses.
External linksCell / PubMed:32937107 / PubMed Central
MethodsEM (subtomogram averaging) / X-ray diffraction
Resolution1.902 - 15.6 Å
Structure data

11236

6zjm

EMDB-11236: Reconstruction of Tula virus surface glycoprotein lattice
PDB-6zjm: Atomic model of Andes virus glycoprotein spike tetramer generated by fitting into a Tula virus reconstruction
Method: EM (subtomogram averaging) / Resolution: 11.4 Å

EMDB-4867:
Sub-tomogram averaging of Tula virus glycoprotein spike
Method: EM (subtomogram averaging) / Resolution: 15.6 Å

PDB-6y5f:
Crystal structure of the envelope glycoprotein prefusion complex of Andes virus - Mutant H953F
Method: X-RAY DIFFRACTION / Resolution: 3.2 Å

PDB-6y5w:
Crystal structure of the envelope glycoprotein complex of Andes virus in a near postfusion conformation
Method: X-RAY DIFFRACTION / Resolution: 2.55 Å

PDB-6y62:
Crystal structure of the envelope glycoprotein complex of Maporal virus in a prefusion conformation
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-6y68:
Structure of Maporal virus envelope glycoprotein Gc in postfusion conformation
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-6y6p:
Structure of Hantaan virus envelope glycoprotein Gn
Method: X-RAY DIFFRACTION / Resolution: 1.938 Å

PDB-6y6q:
Structure of Andes virus envelope glycoprotein Gc in postfusion conformation
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

PDB-6yrb:
Crystal structure of the tetramerization domain of the glycoprotein Gn (Andes virus) at pH 7.5
Method: X-RAY DIFFRACTION / Resolution: 2.351 Å

PDB-6yrq:
Crystal structure of the tetramerization domain of the glycoprotein Gn (Andes virus) at pH 4.6
Method: X-RAY DIFFRACTION / Resolution: 1.902 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-PO4:
PHOSPHATE ION

ChemComp-HOH:
WATER

ChemComp-CD:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-IOD:
IODIDE ION

ChemComp-MPD:
(4S)-2-METHYL-2,4-PENTANEDIOL / precipitant*YM

Source
  • tula orthohantavirus
  • andes orthohantavirus
  • maporal virus
  • hantaan orthohantavirus
  • drosophila melanogaster (fruit fly)
KeywordsVIRAL PROTEIN / class-II fusion protein hantavirus bunyavirus prefusion complex / class-II fusion protein hantavirus bunyavirus / prefusion complex / postfusion conformation / Hantavirus / Tula / Andes / TULV / ANDV / glycoprotein / lattice / spike / fusion protein

+
About Yorodumi Papers

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242)：Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi Papers

Database of articles cited by EMDB/PDB/SASBDB data

  • Database of articles cited by EMDB, PDB, and SASBDB entries
  • Using PubMed data

Related info.:EMDB / PDB / SASBDB / Yorodumi / EMN Papers / Changes in new EM Navigator and Yorodumi

Read more