Evidence map›Paper›PMID 26039169›Full record

ArticleBiophysical journal2015

Crystal structures of the L1, L2, N, and O states of pharaonis halorhodopsin.

Tsutomu Kouyama, Haruki Kawaguchi, Taichi Nakanishi, Hiroki Kubo, Midori Murakami

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Article
  3. Mechanisms of inward transmembrane proton translocation.Nature structural & molecular biology · 2023
    Article
  4. Article
  5. Article
  6. Article
  7. Microbial Rhodopsins.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  8. Crystallization of Microbial Rhodopsins.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  9. Functional Mechanism of ClAdvances in experimental medicine and biology · 2021
    Review
  10. Review
  11. Unique ClBiophysics and physicobiology · 2021
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
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 1 institution in 1 country.

Tsutomu KouyamaDepartment of Physics, Graduate School of Science, Nagoya University, Nagoya, Japan; RIKEN Harima Branch, 1-1-1, Kouto, Sayo, Hyogo, Japan. Electronic address: kouyama@bio.phys.nagoya-u.ac.jp.
Haruki KawaguchiDepartment of Physics, Graduate School of Science, Nagoya University, Nagoya, Japan.
Taichi NakanishiDepartment of Physics, Graduate School of Science, Nagoya University, Nagoya, Japan.
Hiroki KuboDepartment of Physics, Graduate School of Science, Nagoya University, Nagoya, Japan.
Midori MurakamiDepartment of Physics, Graduate School of Science, Nagoya University, Nagoya, Japan.
Nagoya University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Halorhodopsin from Natronomonas pharaonis (pHR) functions as a light-driven halide ion pump. In the presence of halide ions, the photochemical reaction of pHR is described by the scheme: K→ L1 → L2 → N → O → pHR' → pHR. Here, we report light-induced structural changes of the pHR-bromide complex observed in the C2 crystal. In the L1-to-L2 transition, the bromide ion that initially exists in the extracellular vicinity of retinal moves across the retinal Schiff base. Upon the formation of the N state with a bromide ion bound to the cytoplasmic vicinity of the retinal Schiff base, the cytoplasmic half of helix F moves outward to create a water channel in the cytoplasmic interhelical space, whereas the extracellular half of helix C moves inward. During the transition from N to an N-like reaction state with retinal assuming the 13-cis/15-syn configuration, the translocated bromide ion is released into the cytoplasmic medium. Subsequently, helix F relaxes into its original conformation, generating the O state. Anion uptake from the extracellular side occurs when helix C relaxes into its original conformation. These structural data provide insight into the structural basis of unidirectional anion transport.

Indexed as

HalobacteriaceaeCrystallography, X-RayHalorhodopsinsKineticsLightModels, MolecularProtein MultimerizationProtein Structure, QuaternaryRetinaldehydeTemperatureHalorhodopsinsRetinaldehyde

Identifiers

PMID26039169
PMCPMC4457492
OpenAlexW2075893112

What OpenQuestion holds

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LicenceCC BY-NC-ND
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.