Evidence map›Paper›PMID 11452084›Full record

ArticleScience (New York, N.Y.)2001

Crystal structure of sensory rhodopsin II at 2.4 angstroms: insights into color tuning and transducer interaction.

H Luecke, B Schobert, J K Lanyi, E N Spudich, J L Spudich

Abstract read
In one paragraph

Article in Science (New York, N.Y.), 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers.

0numbers the graph read from it
0cells of the map it votes in
97citing 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

97 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Evolution of the Automatic Rhodopsin Modeling (ARM) Protocol.Topics in current chemistry (Cham) · 2022
    Review
  7. Crystallization of Microbial Rhodopsins.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  8. Review
  9. Article
  10. Review
  11. A distinct lineage of giant viruses brings a rhodopsin photosystem to unicellular marine predators.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  12. Article
  13. Toward the Optical Cochlear Implant.Cold Spring Harbor perspectives in medicine · 2019
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Article

37 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.

H LueckeDepartment of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697, USA. hudel@uci.edu
B Schobert
J K Lanyi
E N Spudich
J L Spudich

Funding

Structure/Function of Microbial Sensory RhodopsinsR01GM027750 · NIGMS · YESHIVA UNIVERSITY · PI SPUDICH, JOHN LEE · 1985 to 2020
$6.6M
MECHANISM OF CHLORIDE TRANSPORT BY HALORHODOPSINR01GM029498 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI LANYI, JANOS K · 1985 to 2013
$2.1M
STRUCTURAL STUDIES OF THE BACTERIORHODOPSIN PHOTOCYCLER01GM059970 · NIGMS · UNIVERSITY OF CALIFORNIA IRVINE · PI LUECKE, HARTMUT · 1999 to 2002
$746k
NIGMS NIH HHS R01 GM027750NIGMS NIH HHS R01 GM029498NIGMS NIH HHS R01 GM059970NIGMS NIH HHS R01-GM27750NIGMS NIH HHS R01-GM29498NIGMS NIH HHS R01-GM59970
6 · The paper itself

Abstract

We report an atomic-resolution structure for a sensory member of the microbial rhodopsin family, the phototaxis receptor sensory rhodopsin II (NpSRII), which mediates blue-light avoidance by the haloarchaeon Natronobacterium pharaonis. The 2.4 angstrom structure reveals features responsible for the 70- to 80-nanometer blue shift of its absorption maximum relative to those of haloarchaeal transport rhodopsins, as well as structural differences due to its sensory, as opposed to transport, function. Multiple factors appear to account for the spectral tuning difference with respect to bacteriorhodopsin: (i) repositioning of the guanidinium group of arginine 72, a residue that interacts with the counterion to the retinylidene protonated Schiff base; (ii) rearrangement of the protein near the retinal ring; and (iii) changes in tilt and slant of the retinal polyene chain. Inspection of the surface topography reveals an exposed polar residue, tyrosine 199, not present in bacteriorhodopsin, in the middle of the membrane bilayer. We propose that this residue interacts with the adjacent helices of the cognate NpSRII transducer NpHtrII.

Indexed as

CarotenoidsArchaeal ProteinsArginineBacteriorhodopsinsBinding SitesColorCrystallography, X-RayElectron Spin Resonance SpectroscopyHydrogen BondingIon TransportLightModels, MolecularNatronobacteriumProtein ConformationProtein Structure, SecondaryProtonsArchaeal ProteinsArginineBacteriorhodopsinsCarotenoidsHtrII protein, Natronobacterium pharaonisphototaxis receptor sensory rhodopsin II, Natronobacterium pharaonisProtonsRetinaldehydeSchiff BasesTyrosine

Identifiers

PMID11452084
PMCPMC4996266

What OpenQuestion holds

Textmetadata
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.