[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

TitleCryo-electron microscopy of hepatitis B virions reveals variability in envelope capsid interactions.
Journal, issue, pagesEMBO J, Vol. 26, Issue 18, Page 4160-4167, Year 2007
Publish dateSep 19, 2007
AuthorsStefan Seitz / Stephan Urban / Christoph Antoni / Bettina Böttcher /
PubMed AbstractHepatitis B virus (HBV) is a major human pathogen causing about 750,000 deaths per year. The virion consists of a nucleocapsid and an envelope formed by lipids, and three integral membrane proteins. ...Hepatitis B virus (HBV) is a major human pathogen causing about 750,000 deaths per year. The virion consists of a nucleocapsid and an envelope formed by lipids, and three integral membrane proteins. Although we have detailed structural insights into the organization of the HBV core, the arrangement of the envelope in virions and its interaction with the nucleocapsid is elusive. Here we show the ultrastructure of hepatitis B virions purified from patient serum. We identified two morphological phenotypes, which appear as compact and gapped particles with nucleocapsids in distinguishable conformations. The overall structures of these nucleocapsids resemble recombinant cores with two alpha-helical spikes per asymmetric unit. At the charged tips the spikes are contacted by defined protrusions of the envelope proteins, probably via electrostatic interactions. The HBV envelope in the two morphotypes is to some extent variable, but the surface proteins follow a general packing scheme with up to three surface protein dimers per asymmetric unit. The variability in the structure of the envelope indicates that the nucleocapsid does not firmly constrain the arrangement of the surface proteins, but provides a general template for the packing.
External linksEMBO J / PubMed:17762862 / PubMed Central
MethodsEM (single particle)
Resolution22.0 Å
Structure data

EMDB-1399:
Cryo-electron microscopy of hepatitis B virions reveals variability in envelope capsid interactions.
Method: EM (single particle)

EMDB-1400:
Cryo-electron microscopy of hepatitis B virions reveals variability in envelope capsid interactions.
Method: EM (single particle) / Resolution: 22.0 Å

EMDB-1401:
Cryo-electron microscopy of hepatitis B virions reveals variability in envelope capsid interactions.
Method: EM (single particle) / Resolution: 22.0 Å

EMDB-1402:
Cryo-electron microscopy of hepatitis B virions reveals variability in envelope capsid interactions.
Method: EM (single particle) / Resolution: 22.0 Å

EMDB-1403:
Cryo-electron microscopy of hepatitis B virions reveals variability in envelope capsid interactions.
Method: EM (single particle)

EMDB-1404:
Cryo-electron microscopy of hepatitis B virions reveals variability in envelope capsid interactions.
Method: EM (single particle)

EMDB-1405:
Cryo-electron microscopy of hepatitis B virions reveals variability in envelope capsid interactions.
Method: EM (single particle)

EMDB-1406:
Cryo-electron microscopy of hepatitis B virions reveals variability in envelope capsid interactions.
Method: EM (single particle)

EMDB-1407:
Cryo-electron microscopy of hepatitis B virions reveals variability in envelope capsid interactions.
Method: EM (single particle)

EMDB-1408:
Cryo-electron microscopy of hepatitis B virions reveals variability in envelope capsid interactions.
Method: EM (single particle)

+
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