Evidence map›Paper›PMID 11152120›Full record

ArticleProtein science : a publication of the Protein Society2000

Structure of the Ca2+-regulated photoprotein obelin at 1.7 A resolution determined directly from its sulfur substructure.

Z J Liu, E S Vysotski, C J Chen, J P Rose, J Lee, B C Wang

Open access · greenAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.2field-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

35 citing papers in PubMed, 151 citations in OpenAlex.

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  3. Exploring the Light-Emitting Agents inJournal of the American Chemical Society · 2024
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  7. Crystal structure of semisynthetic obelin-v.Protein science : a publication of the Protein Society · 2022
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  8. Phosphorus and sulfur SAD phasing of the nucleic acid-bound DNA-binding domain of interferon regulatory factor 4.Acta crystallographica. Section F, Structural biology communications · 2021
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  9. Unusual shift in the visible absorption spectrum of an active ctenophore photoprotein elucidated by time-dependent density functional theory.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2021
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  12. The hidden treasure in your data: phasing with unexpected weak anomalous scatterers from routine data sets.Acta crystallographica. Section F, Structural biology communications · 2017
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  13. In-vacuum long-wavelength macromolecular crystallography.Acta crystallographica. Section D, Structural biology · 2016
    Article
  14. Review
  15. Multi-crystal native SAD analysis at 6 keV.Acta crystallographica. Section D, Biological crystallography · 2014
    Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. 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

6 authors at 1 institution in 2 countries.

Z J LiuDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens 30602, USA.
E S Vysotski
C J Chen
J P Rose
J Lee
B C Wang
University of Georgia · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The crystal structure of the photoprotein obelin (22.2 kDa) from Obelia longissima has been determined and refined to 1.7 A resolution. Contrary to the prediction of a peroxide, the noncovalently bound substrate, coelenterazine, has only a single oxygen atom bound at the C2-position. The protein-coelenterazine 2-oxy complex observed in the crystals is photo-active because, in the presence of calcium ion, bioluminescence emission within the crystal is observed. This structure represents only the second de novo protein structure determined using the anomalous scattering signal of the sulfur substructure in the crystal. The method used here is theoretically different from that used for crambin in 1981 (4.72 kDa) and represents a significant advancement in protein crystal structure determination.

Indexed as

ImidazolesAequorinAmino Acid SequenceCalciumCrystallography, X-RayLuminescent ProteinsModels, MolecularMolecular Sequence DataOxygenProtein BindingProtein ConformationProtein Structure, SecondaryPyrazinesRecombinant ProteinsSequence Homology, Amino AcidSulfurAequorinCalciumcoelenterazineImidazolesLuminescent ProteinsobelinOxygenPyrazinesRecombinant ProteinsSulfur

Identifiers

PMID11152120
PMCPMC2144499
OpenAlexW2114221077

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.