Evidence map›Paper›PMID 33888705›Full record

ArticleNature communications2021

Crystal structures of an E1-E2-ubiquitin thioester mimetic reveal molecular mechanisms of transthioesterification.

Lingmin Yuan, Zongyang Lv, Melanie J Adams, Shaun K Olsen

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

21 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Covalent inhibition ofiScience · 2025
    Article
  10. UtilizingJournal of developmental biology · 2025
    Review
  11. Chemical Tools for Probing the Ub/Ubl Conjugation Cascades.Chembiochem : a European journal of chemical biology · 2025
    Review
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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

4 authors at 1 institution in 1 country.

Lingmin YuanDepartment of Biochemistry & Molecular Biology and Hollings Cancer Center, Medical University of South Carolina, Charleston, SC, USA.
Zongyang LvDepartment of Biochemistry & Molecular Biology and Hollings Cancer Center, Medical University of South Carolina, Charleston, SC, USA.
Melanie J AdamsDepartment of Biochemistry & Molecular Biology and Hollings Cancer Center, Medical University of South Carolina, Charleston, SC, USA.ORCID 0000-0002-8210-1096
Shaun K OlsenDepartment of Biochemistry & Molecular Biology and Hollings Cancer Center, Medical University of South Carolina, Charleston, SC, USA. olsens@uthscsa.edu.ORCID 0000-0002-1265-7101
Medical University of South Carolina · US

Funding

TISSUE CULTURE---COREP30CA054174 · NCI · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI Lei Zheng · 1991 to 2026
$59.1M
User Training and OutreachP30GM124165 · NIGMS · CORNELL UNIVERSITY · PI MALCOLM S. CAPEL · 2018 to 2026
$34.2M
Structural Biology of the Ubiquitin Conjugation SystemR01GM115568 · NIGMS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI OLSEN, SHAUN · 2015 to 2023
$2.7M
Structure and Function of the Essential Cell Cycle Regulator Cdc34R01GM128731 · NIGMS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI Shaun Olsen · 2019 to 2026
$2.5M
Pixel Array Detector for Macromolecular CrystallographyS10OD021527 · OD · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2016 to 2016
$2.0M
NCI NIH HHS P30 CA054174NIGMS NIH HHS P30 GM124165NIGMS NIH HHS R01 GM115568NIGMS NIH HHS R01 GM128731NIH HHS S10 OD021527
6 · The paper itself

Abstract

E1 enzymes function as gatekeepers of ubiquitin (Ub) signaling by catalyzing activation and transfer of Ub to tens of cognate E2 conjugating enzymes in a process called E1-E2 transthioesterification. The molecular mechanisms of transthioesterification and the overall architecture of the E1-E2-Ub complex during catalysis are unknown. Here, we determine the structure of a covalently trapped E1-E2-ubiquitin thioester mimetic. Two distinct architectures of the complex are observed, one in which the Ub thioester (Ub(t)) contacts E1 in an open conformation and another in which Ub(t) instead contacts E2 in a drastically different, closed conformation. Altogether our structural and biochemical data suggest that these two conformational states represent snapshots of the E1-E2-Ub complex pre- and post-thioester transfer, and are consistent with a model in which catalysis is enhanced by a Ub(t)-mediated affinity switch that drives the reaction forward by promoting productive complex formation or product release depending on the conformational state.

Indexed as

Catalytic DomainCrystallography, X-RayEsterificationModels, MolecularRecombinant ProteinsSaccharomyces cerevisiae ProteinsUbiquitinUbiquitin-Activating EnzymesUbiquitinationUbiquitin-Conjugating EnzymesCDC34 protein, S cerevisiaeRecombinant ProteinsSaccharomyces cerevisiae ProteinsUba1 protein, S cerevisiaeUbiquitinUbiquitin-Activating EnzymesUbiquitin-Conjugating Enzymes

Identifiers

PMID33888705
PMCPMC8062481
OpenAlexW3153178034

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.