Evidence map›Paper›PMID 21892138›Full record

ArticleThe EMBO journal2011

Crystal structures of an archaeal class II DNA photolyase and its complex with UV-damaged duplex DNA.

Stephan Kiontke, Yann Geisselbrecht, Richard Pokorny, Thomas Carell, Alfred Batschauer, Lars-Oliver Essen

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed, 1 pooled it
9.4field-weighted citation impact, top 2% 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

46 citing papers in PubMed, 1 synthesis or guideline pooled it, 95 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Elucidation of a distinct photoreduction pathway in class IIProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. A structural decryption of cryptochromes.Frontiers in chemistry · 2024
    Review
  9. Article
  10. Photolyase Production and Current Applications: A Review.Molecules (Basel, Switzerland) · 2022
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Formation and Recognition of UV-Induced DNA Damage within Genome Complexity.International journal of molecular sciences · 2020
    Review
  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 2 institutions in 1 country.

Stephan KiontkeFaculty of Chemistry, Department of Biochemistry, Philipps University, Marburg, Germany.
Yann Geisselbrecht
Richard Pokorny
Thomas Carell
Alfred Batschauer
Lars-Oliver Essen
Philipps University of Marburg · DECenter for Integrated Protein Science Munich · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Class II photolyases ubiquitously occur in plants, animals, prokaryotes and some viruses. Like the distantly related microbial class I photolyases, these enzymes repair UV-induced cyclobutane pyrimidine dimer (CPD) lesions within duplex DNA using blue/near-UV light. Methanosarcina mazei Mm0852 is a class II photolyase of the archaeal order of Methanosarcinales, and is closely related to plant and metazoan counterparts. Mm0852 catalyses light-driven DNA repair and photoreduction, but in contrast to class I enzymes lacks a high degree of binding discrimination between UV-damaged and intact duplex DNA. We solved crystal structures of Mm0852, the first one for a class II photolyase, alone and in complex with CPD lesion-containing duplex DNA. The lesion-binding mode differs from other photolyases by a larger DNA-binding site, and an unrepaired CPD lesion is found flipped into the active site and recognized by a cluster of five water molecules next to the bound 3'-thymine base. Different from other members of the photolyase-cryptochrome family, class II photolyases appear to utilize an unusual, conserved tryptophane dyad as electron transfer pathway to the catalytic FAD cofactor.

Indexed as

DNA Breaks, Double-StrandedArchaeaCrystallography, X-RayDeoxyribodipyrimidine Photo-LyaseDNA, ArchaealDNA DamageMethanosarcinaModels, BiologicalModels, MolecularPhylogenyProtein Interaction Domains and MotifsProtein Interaction MappingProtein Structure, QuaternaryProtein Structure, SecondarySequence Homology, Amino AcidUltraviolet RaysDeoxyribodipyrimidine Photo-LyaseDNA, Archaeal

Identifiers

PMID21892138
PMCPMC3230371
OpenAlexW1844128776

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.