Evidence map›Paper›PMID 24980798›Full record

ArticleStructure (London, England : 1993)2014

Lateral opening and exit pore formation are required for BamA function.

Nicholas Noinaj, Adam J Kuszak, Curtis Balusek, James C Gumbart, Susan K Buchanan

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 136 papers.

0numbers the graph read from it
0cells of the map it votes in
136citing papers in PubMed
15.2field-weighted citation impact, top 1% 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

136 citing papers in PubMed, 196 citations in OpenAlex.

  1. Review
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  15. Native β-barrel substrates pass through two shared intermediates during folding on the BAM complex.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Immunodominant extracellular loops ofbioRxiv : the preprint server for biology · 2024
    Article

76 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 at 2 institutions in 1 country.

Nicholas NoinajLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Adam J KuszakLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Curtis BalusekSchool of Physics, Georgia Institute of Technology, Atlanta, GA 30332, USA.
James C GumbartSchool of Physics, Georgia Institute of Technology, Atlanta, GA 30332, USA.
Susan K BuchananLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA. Electronic address: skbuchan@helix.nih.gov.
National Institutes of Health · USGeorgia Institute of Technology · US

Funding

structural characterization of bacterial secretion channelsZIADK036139 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BUCHANAN, SUSAN · 2009 to 2025
$19.3M
System-Level Simulation of a Bioenergetic MembraneR01GM067887 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI TAJKHORSHID, EMAD · 2003 to 2018
$4.0M
Innovative Supercomputing for Breakthrough Molecular DynamicsRC2GM093307 · NIGMS · CARNEGIE-MELLON UNIVERSITY · PI DITTRICH, MARKUS · 2009 to 2010
$2.7M
COMBATING INFECTION THROUGH ATOMIC-SCALE MODELING OF UNIQUE BACTERIAL SYSTEMSK22AI100927 · NIAID · GEORGIA INSTITUTE OF TECHNOLOGY · PI GUMBART, JAMES C. · 2013 to 2014
$269k
Intramural NIH HHS ZIA DK036139NIAID NIH HHS K22 AI100927NIAID NIH HHS K22-AI100927NIGMS NIH HHS R01 GM067887NIGMS NIH HHS R01-GM67887NIGMS NIH HHS RC2 GM093307NIGMS NIH HHS RC2GM093307
6 · The paper itself

Abstract

The outer membrane of Gram-negative bacteria is replete with a host of β-barrel outer membrane proteins (OMPs). Despite serving a variety of essential functions, including immune response evasion, the exact mechanism of OMP folding and membrane insertion remains largely unclear. The β-barrel assembly machinery complex is required for OMP biogenesis. Crystal structures and molecular dynamics (MD) simulations of the central and essential component, BamA, suggest a mechanism involving lateral opening of its barrel domain. MD simulations reported here reveal an additional feature of BamA: a substrate exit pore positioned above the lateral opening site. Disulfide crosslinks that prevent lateral opening and exit pore formation result in a loss of BamA function, which can be fully rescued by the reductant tris(2-carboxyethyl)phosphine. These data provide strong evidence that lateral opening and exit pore formation are required for BamA function.

Indexed as

Bacterial Outer Membrane ProteinsCross-Linking ReagentsDisulfidesEscherichia coliEscherichia coli ProteinsMolecular Dynamics SimulationMutationPhosphinesProtein FoldingProtein Structure, TertiaryBacterial Outer Membrane ProteinsBamA protein, E coliCross-Linking ReagentsDisulfidesEscherichia coli ProteinsPhosphinestris(2-carboxyethyl)phosphine

Identifiers

PMID24980798
PMCPMC4100585
OpenAlexW2058485193

What OpenQuestion holds

Textmetadata
LicenceTDM
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.