Evidence map›Paper›PMID 31582852›Full record

ArticleNature structural & molecular biology2019

Cryo-EM structure of the ClpXP protein degradation machinery.

Christos Gatsogiannis, Dora Balogh, Felipe Merino, Stephan A Sieber, Stefan Raunser

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
5.0field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

60 citing papers in PubMed, 92 citations in OpenAlex.

  1. Regulation of cellular proteostasis via mitochondrial protein import.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Christos Gatsogiannis *Department of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, Germany.ORCID http://orcid.org/0000-0002-4922-4545
Dora Balogh *Department of Chemistry, Chair of Organic Chemistry II, Center for Integrated Protein Science (CIPSM), Technische Universität München, Garching, Germany.ORCID http://orcid.org/0000-0003-2071-6498
Felipe MerinoDepartment of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, Germany.ORCID http://orcid.org/0000-0003-4166-8747
Stephan A SieberDepartment of Chemistry, Chair of Organic Chemistry II, Center for Integrated Protein Science (CIPSM), Technische Universität München, Garching, Germany. stephan.sieber@tum.de.ORCID http://orcid.org/0000-0002-9400-906X
Stefan RaunserDepartment of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, Germany. stefan.raunser@mpi-dortmund.mpg.de.ORCID http://orcid.org/0000-0001-9373-3016
Max Planck Institute of Molecular Physiology · DECenter for Integrated Protein Science Munich · DE

Funding

European Research Council 615984
6 · The paper itself

Abstract

The ClpXP machinery is a two-component protease complex that performs targeted protein degradation in bacteria and mitochondria. The complex consists of the AAA+ chaperone ClpX and the peptidase ClpP. The hexameric ClpX utilizes the energy of ATP binding and hydrolysis to engage, unfold and translocate substrates into the catalytic chamber of tetradecameric ClpP, where they are degraded. Formation of the complex involves a symmetry mismatch, because hexameric AAA+ rings bind axially to the opposing stacked heptameric rings of the tetradecameric ClpP. Here we present the cryo-EM structure of ClpXP from Listeria monocytogenes. We unravel the heptamer-hexamer binding interface and provide novel insight into the ClpX-ClpP cross-talk and activation mechanism. Comparison with available crystal structures of ClpP and ClpX in different states allows us to understand important aspects of the complex mode of action of ClpXP and provides a structural framework for future pharmacological applications.

Indexed as

Bacterial ProteinsCryoelectron MicroscopyEndopeptidase ClpEnzyme ActivationListeria monocytogenesListeriosisModels, MolecularProtein MultimerizationProteolysisBacterial ProteinsEndopeptidase Clp

Identifiers

PMID31582852
PMCPMC6783313
OpenAlexW2977531116

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.