[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

TitleTime-resolved cryo-EM visualizes ribosomal translocation with EF-G and GTP.
Journal, issue, pagesNat Commun, Vol. 12, Issue 1, Page 7236, Year 2021
Publish dateDec 13, 2021
AuthorsChristine E Carbone / Anna B Loveland / Howard B Gamper / Ya-Ming Hou / Gabriel Demo / Andrei A Korostelev /
PubMed AbstractDuring translation, a conserved GTPase elongation factor-EF-G in bacteria or eEF2 in eukaryotes-translocates tRNA and mRNA through the ribosome. EF-G has been proposed to act as a flexible motor that ...During translation, a conserved GTPase elongation factor-EF-G in bacteria or eEF2 in eukaryotes-translocates tRNA and mRNA through the ribosome. EF-G has been proposed to act as a flexible motor that propels tRNA and mRNA movement, as a rigid pawl that biases unidirectional translocation resulting from ribosome rearrangements, or by various combinations of motor- and pawl-like mechanisms. Using time-resolved cryo-EM, we visualized GTP-catalyzed translocation without inhibitors, capturing elusive structures of ribosome•EF-G intermediates at near-atomic resolution. Prior to translocation, EF-G binds near peptidyl-tRNA, while the rotated 30S subunit stabilizes the EF-G GTPase center. Reverse 30S rotation releases Pi and translocates peptidyl-tRNA and EF-G by ~20 Å. An additional 4-Å translocation initiates EF-G dissociation from a transient ribosome state with highly swiveled 30S head. The structures visualize how nearly rigid EF-G rectifies inherent and spontaneous ribosomal dynamics into tRNA-mRNA translocation, whereas GTP hydrolysis and Pi release drive EF-G dissociation.
External linksNat Commun / PubMed:34903725 / PubMed Central
MethodsEM (single particle)
Resolution2.9 - 3.9 Å
Structure data

EMDB-25405, PDB-7ss9:
Late translocation intermediate with EF-G partially dissociated (Structure V)
Method: EM (single particle) / Resolution: 3.9 Å

EMDB-25407, PDB-7ssd:
Mid translocation intermediate with EF-G bound with GDP (Structure IV)
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-25409, PDB-7ssl:
Pre translocation intermediate with EF-G bound to GDP and Pi (Structure III)
Method: EM (single particle) / Resolution: 3.8 Å

EMDB-25410, PDB-7ssn:
Pre translocation 70S ribosome with A/P* and P/E tRNA (Structure II-B)
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-25411, PDB-7sso:
Pre translocation 70S ribosome with A/A and P/E tRNA (Structure II-A)
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-25415, PDB-7ssw:
Late translocation intermediate with EF-G dissociated (Structure VI)
Method: EM (single particle) / Resolution: 3.8 Å

EMDB-25418, PDB-7st2:
Post translocation, non-rotated 70S ribosome with EF-G dissociated (Structure VII)
Method: EM (single particle) / Resolution: 2.9 Å

EMDB-25420, PDB-7st6:
Pre translocation, non-rotated 70S ribosome (Structure I)
Method: EM (single particle) / Resolution: 3.0 Å

EMDB-25421, PDB-7st7:
Pre translocation intermediate stalled with viomycin and bound with EF-G in a GDP and Pi state (Structure III-vio)
Method: EM (single particle) / Resolution: 3.2 Å

Chemicals

ChemComp-GDP:
GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying molecule*YM / Guanosine diphosphate

ChemComp-PO4:
PHOSPHATE ION / Phosphate

ChemComp-FME:
N-FORMYLMETHIONINE / N-Formylmethionine

ChemComp-PRO:
PROLINE / Proline

Source
  • escherichia coli k-12 (bacteria)
  • escherichia coli 113303 (bacteria)
  • streptomyces californicus (bacteria)
KeywordsRIBOSOME / EF-G / GTP / Translocation / GDP / Hybrid / Classical / RIBOSOME/ANTIBIOTIC / Ribosome-Antibiotic complex / Viomycin

+
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