Evidence map›Paper›PMID 25310236›Full record

ArticleeLife2014

A structural mechanism for bacterial autotransporter glycosylation by a dodecameric heptosyltransferase family.

Qing Yao, Qiuhe Lu, Xiaobo Wan, Feng Song, Yue Xu, Mo Hu, Alla Zamyatina, Xiaoyun Liu, Niu Huang, Ping Zhu and 1 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

16 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. 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

11 authors at 5 institutions in 2 countries.

Qing YaoDr Feng Shao's Laboratory, National Institute of Biological Sciences, Beijing, China.
Qiuhe LuDr Feng Shao's Laboratory, National Institute of Biological Sciences, Beijing, China.
Xiaobo WanDr Niu Huang's Laboratory, National Institute of Biological Sciences, Beijing, China.
Feng SongNational Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.
Yue XuDr Feng Shao's Laboratory, National Institute of Biological Sciences, Beijing, China.
Mo HuInstitute of Analytic Chemistry, College of Chemistry and Molecular Engineering, Peking University, Beijing, China.
Alla ZamyatinaDepartment of Chemistry, University of Natural Resources and Life Sciences, Vienna, Austria.
Xiaoyun LiuInstitute of Analytic Chemistry, College of Chemistry and Molecular Engineering, Peking University, Beijing, China.
Niu HuangDr Niu Huang's Laboratory, National Institute of Biological Sciences, Beijing, China.
Ping ZhuNational Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.
Feng ShaoDr Feng Shao's Laboratory, National Institute of Biological Sciences, Beijing, China.
National Institute of Biological Sciences, Beijing · CNPeking University · CNBOKU University · ATChinese Academy of Sciences · CNInstitute of Biophysics · CN

Funding

Howard Hughes Medical Institute 55007431
6 · The paper itself

Abstract

A large group of bacterial virulence autotransporters including AIDA-I from diffusely adhering E. coli (DAEC) and TibA from enterotoxigenic E. coli (ETEC) require hyperglycosylation for functioning. Here we demonstrate that TibC from ETEC harbors a heptosyltransferase activity on TibA and AIDA-I, defining a large family of bacterial autotransporter heptosyltransferases (BAHTs). The crystal structure of TibC reveals a characteristic ring-shape dodecamer. The protomer features an N-terminal β-barrel, a catalytic domain, a β-hairpin thumb, and a unique iron-finger motif. The iron-finger motif contributes to back-to-back dimerization; six dimers form the ring through β-hairpin thumb-mediated hand-in-hand contact. The structure of ADP-D-glycero-β-D-manno-heptose (ADP-D,D-heptose)-bound TibC reveals a sugar transfer mechanism and also the ligand stereoselectivity determinant. Electron-cryomicroscopy analyses uncover a TibC-TibA dodecamer/hexamer assembly with two enzyme molecules binding to one TibA substrate. The complex structure also highlights a high efficient hyperglycosylation of six autotransporter substrates simultaneously by the dodecamer enzyme complex.

Indexed as

Protein MultimerizationAdhesins, Escherichia coliAmino Acid MotifsBacterial AdhesionBiocatalysisCryoelectron MicroscopyCrystallography, X-RayEscherichia coliEscherichia coli ProteinsGlycosylationGlycosyltransferasesHeLa CellsHeptosesHumansLigandsModels, MolecularAdhesins, Escherichia coliAIDA-I protein, E coliEscherichia coli ProteinsGlycosyltransferasesHeptosesheptosyltransferaseLigandsTibA protein, E colibacterial autotransportersbacterial pathogenesisbiophysicscryo-EME. colienzyme catalysisenzyme complexglycosyltransferaseinfectious diseasemicrobiologystructural biology

Identifiers

PMID25310236
PMCPMC4358343
OpenAlexW2167501991

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.