[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

TitleStructures of the ATP-fueled ClpXP proteolytic machine bound to protein substrate.
Journal, issue, pagesElife, Vol. 9, Year 2020
Publish dateFeb 28, 2020
AuthorsXue Fei / Tristan A Bell / Simon Jenni / Benjamin M Stinson / Tania A Baker / Stephen C Harrison / Robert T Sauer /
PubMed AbstractClpXP is an ATP-dependent protease in which the ClpX AAA+ motor binds, unfolds, and translocates specific protein substrates into the degradation chamber of ClpP. We present cryo-EM studies of the ...ClpXP is an ATP-dependent protease in which the ClpX AAA+ motor binds, unfolds, and translocates specific protein substrates into the degradation chamber of ClpP. We present cryo-EM studies of the enzyme that show how asymmetric hexameric rings of ClpX bind symmetric heptameric rings of ClpP and interact with protein substrates. Subunits in the ClpX hexamer assume a spiral conformation and interact with two-residue segments of substrate in the axial channel, as observed for other AAA+ proteases and protein-remodeling machines. Strictly sequential models of ATP hydrolysis and a power stroke that moves two residues of the substrate per translocation step have been inferred from these structural features for other AAA+ unfoldases, but biochemical and single-molecule biophysical studies indicate that ClpXP operates by a probabilistic mechanism in which five to eight residues are translocated for each ATP hydrolyzed. We propose structure-based models that could account for the functional results.
External linksElife / PubMed:32108573 / PubMed Central
MethodsEM (single particle)
Resolution3.19 - 4.28 Å
Structure data

EMDB-20406, PDB-6po1:
ClpX-ClpP complex bound to substrate and ATP-gamma-S, class 4
Method: EM (single particle) / Resolution: 4.2 Å

EMDB-20408, PDB-6po3:
ClpX-ClpP complex bound to substrate and ATP-gamma-S, class 3
Method: EM (single particle) / Resolution: 4.28 Å

EMDB-20412, PDB-6pod:
ClpX-ClpP complex bound to substrate and ATP-gamma-S, class 2
Method: EM (single particle) / Resolution: 4.05 Å

EMDB-20418, PDB-6pos:
ClpX-ClpP complex bound to substrate and ATP-gamma-S, class 1
Method: EM (single particle) / Resolution: 4.12 Å

EMDB-20419, PDB-6pp5:
ClpX in ClpX-ClpP complex bound to substrate and ATP-gamma-S, class 4
Method: EM (single particle) / Resolution: 3.98 Å

EMDB-20420, PDB-6pp6:
ClpX in ClpX-ClpP complex bound to substrate and ATP-gamma-S, class 3
Method: EM (single particle) / Resolution: 4.28 Å

EMDB-20421, PDB-6pp7:
ClpX in ClpX-ClpP complex bound to substrate and ATP-gamma-S, class 2
Method: EM (single particle) / Resolution: 4.05 Å

EMDB-20422, PDB-6pp8:
ClpX in ClpX-ClpP complex bound to substrate and ATP-gamma-S, class 1
Method: EM (single particle) / Resolution: 4.12 Å

EMDB-20434, PDB-6ppe:
ClpP and ClpX IGF loop in ClpX-ClpP complex with D7 symmetry
Method: EM (single particle) / Resolution: 3.19 Å

Chemicals

ChemComp-AGS:
PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / ATP-gamma-S, energy-carrying molecule analogue*YM

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsCHAPERONE / Protein degradation / AAA+ protease complex

+
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