Evidence map›Paper›PMID 40588486›Full record

ArticleNature chemical biology2026

Structure and mechanism of an actin-dependent bacterial phosphoryl AMPylase.

Tao-Tao Chen, Qiuhua Lu, Si-Ru Zheng, Jiaqi Fu, Jing Chen, Lina Kang, Juhong Wu, Jiwei Luo, Jiangyang Tong, Siying Li and 7 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature chemical biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Crystal structure of theVirulence · 2026
    Article
  2. Article
  3. Article
  4. Crystal structure of thebioRxiv : the preprint server for biology · 2025
    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

17 authors.

Tao-Tao Chen *Key Laboratory of Microbial Pathogenesis and Interventions of Fujian Province University, Key Laboratory of Innate Immune Biology of Fujian Province, Biomedical Research Center of South China, College of Life Sciences, Fujian Normal University, Fuzhou, China.ORCID 0000-0002-0660-2841
Qiuhua Lu *Key Laboratory of Microbial Pathogenesis and Interventions of Fujian Province University, Key Laboratory of Innate Immune Biology of Fujian Province, Biomedical Research Center of South China, College of Life Sciences, Fujian Normal University, Fuzhou, China.
Si-Ru Zheng *Key Laboratory of Microbial Pathogenesis and Interventions of Fujian Province University, Key Laboratory of Innate Immune Biology of Fujian Province, Biomedical Research Center of South China, College of Life Sciences, Fujian Normal University, Fuzhou, China.
Jiaqi Fu *Department of Respiratory Medicine, Center for Infectious Diseases and Pathogen Biology, Key Laboratory of Organ Regeneration and Transplantation of the Ministry of Education, State Key Laboratory for Diagnosis and Treatment of Severe Zoonotic Infectious Diseases, The First Hospital of Jilin University, Changchun, China.ORCID 0000-0003-0081-6133
Jing Chen *Department of Hematology, Fujian Institute of Hematology, Fujian Provincial Key Laboratory on Hematology, Fujian Medical University Union Hospital, Fuzhou, China.
Lina KangKey Laboratory of Microbial Pathogenesis and Interventions of Fujian Province University, Key Laboratory of Innate Immune Biology of Fujian Province, Biomedical Research Center of South China, College of Life Sciences, Fujian Normal University, Fuzhou, China.
Juhong WuCollege of Chemistry, Fuzhou University, Fuzhou, China.ORCID 0009-0009-6442-4594
Jiwei LuoNational Key Laboratory of Agricultural Microbiology, College of Biomedicine and Health, College of Life Science and Technology, Huazhong Agricultural University, Wuhan, China.
Jiangyang TongKey Laboratory of Microbial Pathogenesis and Interventions of Fujian Province University, Key Laboratory of Innate Immune Biology of Fujian Province, Biomedical Research Center of South China, College of Life Sciences, Fujian Normal University, Fuzhou, China.
Siying LiDepartment of Respiratory Medicine, Center for Infectious Diseases and Pathogen Biology, Key Laboratory of Organ Regeneration and Transplantation of the Ministry of Education, State Key Laboratory for Diagnosis and Treatment of Severe Zoonotic Infectious Diseases, The First Hospital of Jilin University, Changchun, China.
Xiangliang LiKey Laboratory of Microbial Pathogenesis and Interventions of Fujian Province University, Key Laboratory of Innate Immune Biology of Fujian Province, Biomedical Research Center of South China, College of Life Sciences, Fujian Normal University, Fuzhou, China.
Shan LiNational Key Laboratory of Agricultural Microbiology, College of Biomedicine and Health, College of Life Science and Technology, Huazhong Agricultural University, Wuhan, China.ORCID 0000-0001-8646-3193
Jinyu LiCollege of Chemistry, Fuzhou University, Fuzhou, China.ORCID 0000-0002-8220-049X
Shaoyuan WangDepartment of Hematology, Fujian Institute of Hematology, Fujian Provincial Key Laboratory on Hematology, Fujian Medical University Union Hospital, Fuzhou, China.
Yue FengBeijing Advanced Innovation Center for Soft Matter Science and Engineering, Beijing Key Laboratory of Bioprocess, State Key Laboratory of Chemical Resource Engineering, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing, China.
Zhao-Qing LuoDepartment of Biological Sciences, Purdue University, West Lafayette, IN, USA. luoz@purdue.edu.ORCID 0000-0001-8890-6621
Songying OuyangKey Laboratory of Microbial Pathogenesis and Interventions of Fujian Province University, Key Laboratory of Innate Immune Biology of Fujian Province, Biomedical Research Center of South China, College of Life Sciences, Fujian Normal University, Fuzhou, China. ouyangsy@fjnu.edu.cn.ORCID 0000-0002-1120-1524

Funding

Effector-mediated Ubiquitin Manipulation in Legionella Pneumophila PathogenesisR01AI127465 · NIAID · PURDUE UNIVERSITY · PI Qing Deng · 2017 to 2026
$3.4M
Foundation for the National Institutes of Health (Foundation for the National Institutes of Health, Inc.) R01AI127465National Natural Science Foundation of China (National Science Foundation of China) 82172287National Natural Science Foundation of China (National Science Foundation of China) 82225028NIAID NIH HHS R01 AI127465
6 · The paper itself

Abstract

The two effectors LnaB and MavL of Legionella pneumophila coordinate the conversion of phosphoribosyl ubiquitin (PR-Ub) released by reversal of ubiquitination induced by members of the SidE effector family into functional Ub. LnaB acts as an actin-dependent phosphoryl AMPylase that converts PR-Ub into ADP-ribosylated (ADPR)-Ub. Catalysis by LnaB requires the conserved SHE motif present in a large family of bacterial toxins. Here we describe a series of structures of LnaB in complex with the cofactor actin and the substrate PR-Ub and ATP. LnaB harbors both adenylyltransferase and ATPase activities, which reveal an adenylylation mechanism involved in a two-step catalytic process. Actin performs a unique activation mechanism that promotes the recruitment of PR-Ub by LnaB to activate LnaB's ATPase activity through interacting with LnaB and PR-Ub. Mechanisms derived from this series of structures covering the process of LnaB action establish an important biochemical basis for protein AMPylation.

Indexed as

ActinsBacterial ProteinsLegionella pneumophilaAdenosine TriphosphateCrystallography, X-RayModels, MolecularNucleotidyltransferasesActinsAdenosine TriphosphateBacterial ProteinsNucleotidyltransferases

Identifiers

PMID40588486
PMCPMC13047714

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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.