[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

TitleStructural basis of the bacterial flagellar motor rotational switching.
Journal, issue, pagesCell Res, Vol. 34, Issue 11, Page 788-801, Year 2024
Publish dateAug 23, 2024
AuthorsJiaxing Tan / Ling Zhang / Xingtong Zhou / Siyu Han / Yan Zhou / Yongqun Zhu /
PubMed AbstractThe bacterial flagellar motor is a huge bidirectional rotary nanomachine that drives rotation of the flagellum for bacterial motility. The cytoplasmic C ring of the flagellar motor functions as the ...The bacterial flagellar motor is a huge bidirectional rotary nanomachine that drives rotation of the flagellum for bacterial motility. The cytoplasmic C ring of the flagellar motor functions as the switch complex for the rotational direction switching from counterclockwise to clockwise. However, the structural basis of the rotational switching and how the C ring is assembled have long remained elusive. Here, we present two high-resolution cryo-electron microscopy structures of the C ring-containing flagellar basal body-hook complex from Salmonella Typhimurium, which are in the default counterclockwise state and in a constitutively active CheY mutant-induced clockwise state, respectively. In both complexes, the C ring consists of four subrings, but is in two different conformations. The CheY proteins are bound into an open groove between two adjacent protomers on the surface of the middle subring of the C ring and interact with the FliG and FliM subunits. The binding of the CheY protein induces a significant upward shift of the C ring towards the MS ring and inward movements of its protomers towards the motor center, which eventually remodels the structures of the FliG subunits and reverses the orientations and surface electrostatic potential of the α helices to trigger the counterclockwise-to-clockwise rotational switching. The conformational changes of the FliG subunits reveal that the stator units on the motor require a relocation process in the inner membrane during the rotational switching. This study provides unprecedented molecular insights into the rotational switching mechanism and a detailed overall structural view of the bacterial flagellar motors.
External linksCell Res / PubMed:39179739 / PubMed Central
MethodsEM (single particle)
Resolution2.75 - 7.4 Å
Structure data

EMDB-37547, PDB-8wht:
Cryo-EM structure of the LP ring within the flagellar motor-hook complex in the CW state
Method: EM (single particle) / Resolution: 2.75 Å

EMDB-37570, PDB-8wiw:
Cryo-EM structure of the flagellar C ring in the CW state
Method: EM (single particle) / Resolution: 5.6 Å

EMDB-37590, PDB-8wjr:
Cryo-EM structure of the MS ring (C34) within the flagellar motor-hook complex in the CW state
Method: EM (single particle) / Resolution: 2.9 Å

EMDB-37594, PDB-8wk3:
Cryo-EM structure of the proximal rod-export apparatus and FlgF within the motor-hook complex in the CW state
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-37595, PDB-8wk4:
Cryo-EM structure of the MS ring with FlgB and FliE within the flagellar motor-hook complex in the CW state.
Method: EM (single particle) / Resolution: 3.7 Å

EMDB-37600, PDB-8wki:
Cryo-EM structure of the distal rod-hook within the flagellar motor-hook complex in the CW state.
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-37601, PDB-8wkk:
Cryo-EM structure of the whole rod with export apparatus and hook within the flagellar motor-hook complex in the CW state.
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-37605, PDB-8wkq:
Cryo-EM structure of the MS ring (C1) with export apparatus and proximal rod within the flagellar motor-hook complex in the CW state.
Method: EM (single particle) / Resolution: 3.8 Å

EMDB-37611, PDB-8wl2:
Cryo-EM structure of the membrane-anchored part of the flagellar motor-hook complex in the CW state.
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-37618, PDB-8wle:
Cryo-EM structure of the LP ring within the flagellar motor-hook complex in the CCW state.
Method: EM (single particle) / Resolution: 3.0 Å

EMDB-37619, PDB-8wlh:
Cryo-EM structure of the proximal rod-export apparatus and FlgF within the motor-hook complex in the CCW state
Method: EM (single particle) / Resolution: 3.7 Å

EMDB-37620, PDB-8wli:
Cryo-EM structure of the MS ring (C34) within the flagellar motor-hook complex in the CCW state
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-37625, PDB-8wln:
Cryo-EM structure of the MS ring with export apparatus and proximal rod within the motor-hook complex in the CCW state
Method: EM (single particle) / Resolution: 4.3 Å

EMDB-37627, PDB-8wlp:
Cryo-EM structure of the distal rod-hook within the flagellar motor-hook complex in the CCW state.
Method: EM (single particle) / Resolution: 3.8 Å

EMDB-37628, PDB-8wlq:
Cryo-EM structure of the whole rod-export apparatus with hook within the flagellar motor-hook complex in the CCW state.
Method: EM (single particle) / Resolution: 3.8 Å

EMDB-37630, PDB-8wlt:
Cryo-EM structure of the membrane-anchored part of the flagellar motor-hook complex in the CCW state
Method: EM (single particle) / Resolution: 4.1 Å

EMDB-37679, PDB-8wo5:
Cryo-EM structure of the intact flagellar motor-hook complex in the CCW state
Method: EM (single particle) / Resolution: 7.4 Å

EMDB-37684, PDB-8woe:
Cryo-EM structure of the intact flagellar motor-hook complex in the CW state
Method: EM (single particle) / Resolution: 4.3 Å

EMDB-38546, PDB-8xp0:
Cryo-EM structure of the protomers of the C ring in the CCW state
Method: EM (single particle) / Resolution: 4.0 Å

EMDB-38547, PDB-8xp1:
Cryo-EM structure of the protomers of the C ring in the CW state
Method: EM (single particle) / Resolution: 4.4 Å

EMDB-39349, PDB-8yjt:
Cryo-EM structure of the flagellar C ring in the CCW state
Method: EM (single particle) / Resolution: 5.9 Å

Source
  • salmonella enterica subsp. enterica serovar typhimurium str. lt2 (bacteria)
KeywordsMOTOR PROTEIN / Flagellum / Flagellar motor / LP ring / C ring / Switch complex / MS ring / Proximal rod / Export apparatus / FlgF / Rod / Hook / CheY / motor / rotation / FliF / FliG / FliM / FliN

+
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