Evidence map›Paper›PMID 15014442›Full record

ArticleThe EMBO journal2004

Structure of the translocator domain of a bacterial autotransporter.

Clasien J Oomen, Peter van Ulsen, Patrick van Gelder, Maya Feijen, Jan Tommassen, Piet Gros

Abstract read
In one paragraph

Article in The EMBO journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 154 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
154citing papers in PubMed, 1 pooled it
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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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

154 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
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  12. The Two TpsB-Like Proteins inJournal of bacteriology · 2021
    Article
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  14. BamA is required for autotransporter secretion.Biochimica et biophysica acta. General subjects · 2020
    Article
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  17. Review
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94 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

6 authors.

Clasien J OomenDepartment of Crystal and Structural Chemistry, Bijvoet Center for Biomolecular Research, Utrecht University, Utrecht, The Netherlands.
Peter van Ulsen
Patrick van Gelder
Maya Feijen
Jan Tommassen
Piet Gros

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Autotransporters are virulence-related proteins of Gram-negative bacteria that are secreted via an outer-membrane-based C-terminal extension, the translocator domain. This domain supposedly is sufficient for the transport of the N-terminal passenger domain across the outer membrane. We present here the crystal structure of the in vitro-folded translocator domain of the autotransporter NalP from Neisseria meningitidis, which reveals a 12-stranded beta-barrel with a hydrophilic pore of 10 x 12.5 A that is filled by an N-terminal alpha-helix. The domain has pore activity in vivo and in vitro. Our data are consistent with the model of passenger-domain transport through the hydrophilic channel within the beta-barrel, and inconsistent with a model for transport through a central channel formed by an oligomer of translocator domains. However, the dimensions of the pore imply translocation of the secreted domain in an unfolded form. An alternative model, possibly covering the transport of folded domains, is that passenger-domain transport involves the Omp85 complex, the machinery required for membrane insertion of outer-membrane proteins, on which autotransporters are dependent.

Indexed as

Amino Acid SequenceCephalosporinsCrystallography, X-RayEscherichia coliGene ExpressionMembrane Transport ProteinsModels, MolecularMolecular Sequence DataNeisseria meningitidisProtein BindingProtein FoldingProtein RenaturationProtein Structure, QuaternaryProtein Structure, SecondaryProtein Structure, TertiaryProtein TransportCephalosporinsMembrane Transport ProteinsNalP protein, Neisseria meningitidisnitrocefinSerine Endopeptidases

Identifiers

PMID15014442
PMCPMC381419

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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.