Evidence map›Paper›PMID 19529756›Full record

ArticlePLoS biology2009

Crystal structure of a yeast aquaporin at 1.15 angstrom reveals a novel gating mechanism.

Gerhard Fischer, Urszula Kosinska-Eriksson, Camilo Aponte-Santamaría, Madelene Palmgren, Cecilia Geijer, Kristina Hedfalk, Stefan Hohmann, Bert L de Groot, Richard Neutze, Karin Lindkvist-Petersson

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
8.9field-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

73 citing papers in PubMed, 185 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Mechanosensitive aquaporins.Biophysical reviews · 2023
    Review
  10. Protein Structure and Modification of Aquaporins.Advances in experimental medicine and biology · 2023
    Article
  11. Article
  12. Aquaporin Gating: A New Twist to Unravel Permeation through Water Channels.International journal of molecular sciences · 2022
    Review
  13. Article
  14. Multiple pore lining residues modulate water permeability of GlpF.Protein science : a publication of the Protein Society · 2022
    Article
  15. Review
  16. Review
  17. Dynamics of Salivary Gland AQP5 under Normal and Pathologic Conditions.International journal of molecular sciences · 2020
    Review
  18. Article
  19. Article
  20. Article

13 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

10 authors at 2 institutions in 2 countries.

Gerhard FischerDepartment of Chemistry, Biochemistry and Biophysics, University of Gothenburg, Göteborg, Sweden.
Urszula Kosinska-Eriksson
Camilo Aponte-Santamaría
Madelene Palmgren
Cecilia Geijer
Kristina Hedfalk
Stefan Hohmann
Bert L de Groot
Richard Neutze
Karin Lindkvist-Petersson
University of Gothenburg · SEMax Planck Society · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aquaporins are transmembrane proteins that facilitate the flow of water through cellular membranes. An unusual characteristic of yeast aquaporins is that they frequently contain an extended N terminus of unknown function. Here we present the X-ray structure of the yeast aquaporin Aqy1 from Pichia pastoris at 1.15 A resolution. Our crystal structure reveals that the water channel is closed by the N terminus, which arranges as a tightly wound helical bundle, with Tyr31 forming H-bond interactions to a water molecule within the pore and thereby occluding the channel entrance. Nevertheless, functional assays show that Aqy1 has appreciable water transport activity that aids survival during rapid freezing of P. pastoris. These findings establish that Aqy1 is a gated water channel. Mutational studies in combination with molecular dynamics simulations imply that gating may be regulated by a combination of phosphorylation and mechanosensitivity.

Indexed as

Ion Channel GatingAquaporinsBiological TransportComputer SimulationCrystallography, X-RayFreezingMicrobial ViabilityModels, MolecularPhosphorylationPichiaProtein Structure, SecondarySpinacia oleraceaStructural Homology, ProteinTyrosineWaterAquaporinsTyrosineWater

Identifiers

PMID19529756
PMCPMC2688079
OpenAlexW1512016817

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.