Evidence map›Paper›PMID 39806067›Full record

ArticleNature chemical biology2025

Transforming an ATP-dependent enzyme into a dissipative, self-assembling system.

Yiying Li, Jie Zhu, Zhiyin Zhang, Jiapeng Wei, Fengbin Wang, Georg Meisl, Tuomas P J Knowles, Edward H Egelman, F Akif Tezcan

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature chemical biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
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

9 authors.

Yiying LiDepartment of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA, USA.ORCID http://orcid.org/0000-0003-3566-6008
Jie ZhuDepartment of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA, USA.
Zhiyin ZhangDepartment of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA, USA.
Jiapeng WeiCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, UK.
Fengbin WangDepartment of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, VA, USA.
Georg MeislCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, UK.ORCID http://orcid.org/0000-0002-6562-7715
Tuomas P J KnowlesCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, UK.ORCID http://orcid.org/0000-0002-7879-0140
Edward H EgelmanDepartment of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, VA, USA.
F Akif TezcanDepartment of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA, USA. tezcan@ucsd.edu.ORCID http://orcid.org/0000-0002-4733-6500

Funding

The Stanford-SLAC CryoEM Center supplementU24GM129541 · NIGMS · STANFORD UNIVERSITY · PI CHIU, WAH, HEDMAN, BRITT · 2018 to 2023
$54.8M
Cryo-EM of Helical Protein and Nucleoprotein Polymers at Near Atomic ResolutionR35GM122510 · NIGMS · UNIVERSITY OF VIRGINIA · PI EDWARD H. EGELMAN · 2017 to 2026
$7.3M
JEOL JEM-1400Plus Transmission Electron MicroscopeS10OD023527 · OD · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI FARQUHAR, MARILYN GIST · 2017 to 2017
$579k
National Science Foundation (NSF) DMR-2004558NIGMS NIH HHS R35 GM122510NIGMS NIH HHS U24 GM129541NIH HHS S10 OD023527U.S. Department of Energy (DOE) DE-SC0003844U.S. Department of Energy (DOE) DE-SC0019288U.S. Department of Health & Human Services | National Institutes of Health (NIH) GM122510
6 · The paper itself

Abstract

Nucleoside triphosphate (NTP)-dependent protein assemblies such as microtubules and actin filaments have inspired the development of diverse chemically fueled molecular machines and active materials but their functional sophistication has yet to be matched by design. Given this challenge, we asked whether it is possible to transform a natural adenosine 5'-triphosphate (ATP)-dependent enzyme into a dissipative self-assembling system, thereby altering the structural and functional mode in which chemical energy is used. Here we report that FtsH (filamentous temperature-sensitive protease H), a hexameric ATPase involved in membrane protein degradation, can be readily engineered to form one-dimensional helical nanotubes. FtsH nanotubes require constant energy input to maintain their integrity and degrade over time with the concomitant hydrolysis of ATP, analogous to natural NTP-dependent cytoskeletal assemblies. Yet, in contrast to natural dissipative systems, ATP hydrolysis is catalyzed by free FtsH protomers and FtsH nanotubes serve to conserve ATP, leading to transient assemblies whose lifetimes can be tuned from days to minutes through the inclusion of external ATPases in solution.

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateHydrolysisModels, MolecularNanotubesAdenosine TriphosphatasesAdenosine Triphosphate

Identifiers

PMID39806067
PMCPMC12124957

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Registered trials

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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.