Evidence map›Paper›PMID 28067918›Full record

ArticleNature structural & molecular biology2017

Structural insights into the secretin translocation channel in the type II secretion system.

Zhaofeng Yan, Meng Yin, Dandan Xu, Yongqun Zhu, Xueming Li

Abstract read
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In one paragraph

Article in Nature structural & molecular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing 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

63 citing papers in PubMed.

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  16. Uncovering the Secretion Systems ofAntibiotics (Basel, Switzerland) · 2023
    Review
  17. Article
  18. Article
  19. Article
  20. Article

3 more citing papers are in PubMed but not listed here.

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.

Zhaofeng YanSchool of Life Sciences, Tsinghua University, Beijing, China.
Meng YinSchool of Life Sciences, Tsinghua University, Beijing, China.
Dandan XuLife Sciences Institute and Innovation Center for Cell Signaling Network, Zhejiang University, Hangzhou, China.
Yongqun ZhuLife Sciences Institute and Innovation Center for Cell Signaling Network, Zhejiang University, Hangzhou, China.
Xueming LiSchool of Life Sciences, Tsinghua University, Beijing, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The secretin GspD of the type II secretion system (T2SS) forms a channel across the outer membrane in Gram-negative bacteria to transport substrates from the periplasm to the extracellular milieu. The lack of an atomic-resolution structure of the GspD channel hinders the investigation of substrate translocation mechanism of T2SS. Here we report cryo-EM structures of two GspD channels (∼1 MDa), from Escherichia coli K12 and Vibrio cholerae, at ∼3 Å resolution. The structures reveal a pentadecameric channel architecture, wherein three rings of GspD N domains form the periplasmic channel. The secretin domain constitutes a novel double β-barrel channel, with at least 60 β-strands in each barrel, and is stabilized by S domains. The outer membrane channel is sealed by β-strand-enriched gates. On the basis of the partially open state captured, we proposed a detailed gate-opening mechanism. Our structures provide a structural basis for understanding the secretin superfamily and the mechanism of substrate translocation in T2SS.

Indexed as

Amino Acid SequenceConserved SequenceCryoelectron MicroscopyEscherichia coliEscherichia coli ProteinsIon Channel GatingModels, MolecularPorinsProtein Conformation, beta-StrandProtein Interaction Domains and MotifsProtein Structure, QuaternarySecretinType II Secretion SystemsEscherichia coli ProteinsGspD protein, E coliPorinsSecretinType II Secretion Systems

Identifiers

PMID28067918

What OpenQuestion holds

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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.