Evidence map›Paper›PMID 19359474›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

Functional motifs in the (6-4) photolyase crystal structure make a comparative framework for DNA repair photolyases and clock cryptochromes.

Kenichi Hitomi, Luciano DiTacchio, Andrew S Arvai, Junpei Yamamoto, Sang-Tae Kim, Takeshi Todo, John A Tainer, Shigenori Iwai, Satchidananda Panda, Elizabeth D Getzoff

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed, 1 pooled it
16.9field-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

61 citing papers in PubMed, 1 synthesis or guideline pooled it, 122 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Plant tolerance mechanisms to DNA-damaging UV stress.Journal of experimental botany · 2025
    Review
  4. Article
  5. Dynamics and mechanism of DNA repair by a bifunctional cryptochrome.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. A structural decryption of cryptochromes.Frontiers in chemistry · 2024
    Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Key interactions with deazariboflavin cofactor for light-driven energy transfer in Xenopus (6-4) photolyase.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2021
    Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Review

1 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 5 institutions in 2 countries.

Kenichi HitomiGraduate School of Engineering Science, Osaka University, Toyonaka, Osaka 560-8531, Japan.
Luciano DiTacchio
Andrew S Arvai
Junpei Yamamoto
Sang-Tae Kim
Takeshi Todo
John A Tainer
Shigenori Iwai
Satchidananda Panda
Elizabeth D Getzoff
Osaka University · JPLawrence Berkeley National Laboratory · USSalk Institute for Biological Studies · USScripps Research Institute · USKyoto University · JP

Funding

Circadian Photoentrainment in MammalsR01EY016807 · NEI · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI PANDA, SATCHIDANANDA · 2007 to 2019
$6.4M
STRUCTURE AND FUNCTION OF METALLOENZYMES FOR DNA REPAIRR01GM046312 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI TAINER, JOHN A. · 1991 to 2012
$5.9M
STRUCTURAL ANALYSIS OF CHROMATICALLY ACTIVE PROTEINSR01GM037684 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI GETZOFF, ELIZABETH D · 1987 to 2009
$3.1M
Temporal transcriptional regulation in liverF32GM082083 · NIGMS · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI DITACCHIO, LUCIANO · 2007 to 2007
$53k
NEI NIH HHS EY016807NEI NIH HHS R01 EY016807NIGMS NIH HHS 1R32GM082083-01NIGMS NIH HHS F32 GM082083NIGMS NIH HHS GM046312NIGMS NIH HHS GM37684NIGMS NIH HHS R01 GM037684NIGMS NIH HHS R01 GM046312
6 · The paper itself

Abstract

Homologous flavoproteins from the photolyase (PHR)/cryptochrome (CRY) family use the FAD cofactor in PHRs to catalyze DNA repair and in CRYs to tune the circadian clock and control development. To help address how PHR/CRY members achieve these diverse functions, we determined the crystallographic structure of Arabidopsis thaliana (6-4) PHR (UVR3), which is strikingly (>65%) similar in sequence to human circadian clock CRYs. The structure reveals a substrate-binding cavity specific for the UV-induced DNA lesion, (6-4) photoproduct, and cofactor binding sites different from those of bacterial PHRs and consistent with distinct mechanisms for activities and regulation. Mutational analyses were combined with this prototypic structure for the (6-4) PHR/clock CRY cluster to identify structural and functional motifs: phosphate-binding and Pro-Lys-Leu protrusion motifs constricting access to the substrate-binding cavity above FAD, sulfur loop near the external end of the Trp electron-transfer pathway, and previously undefined C-terminal helix. Our results provide a detailed, unified framework for investigations of (6-4) PHRs and the mammalian CRYs. Conservation of key residues and motifs controlling FAD access and activities suggests that regulation of FAD redox properties and radical stability is essential not only for (6-4) photoproduct DNA repair, but also for circadian clock-regulating CRY functions. The structural and functional results reported here elucidate archetypal relationships within this flavoprotein family and suggest how PHRs and CRYs use local residue and cofactor tuning, rather than larger structural modifications, to achieve their diverse functions encompassing DNA repair, plant growth and development, and circadian clock regulation.

Indexed as

Circadian RhythmAmino Acid SequenceAnimalsArabidopsisArabidopsis ProteinsBinding SitesConserved SequenceCryptochromesCrystallography, X-RayDeoxyribodipyrimidine Photo-LyaseDNA, PlantDNA RepairFlavoproteinsHydrophobic and Hydrophilic InteractionsMolecular Sequence DataPhosphatesArabidopsis ProteinsCRY1 protein, ArabidopsisCryptochromesDeoxyribodipyrimidine Photo-LyaseDNA, PlantFlavoproteinsPhosphatespyrimidine(6-4)pyrimidone photolyase

Identifiers

PMID19359474
PMCPMC2678464
OpenAlexW2016907186

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.