Evidence map›Paper›PMID 12514126›Full record

ArticleThe EMBO journal2003

The structure of ActVA-Orf6, a novel type of monooxygenase involved in actinorhodin biosynthesis.

Giuliano Sciara, Steven G Kendrew, Adriana E Miele, Neil G Marsh, Luca Federici, Francesco Malatesta, Giuliana Schimperna, Carmelinda Savino, Beatrice Vallone

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
9.0field-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

66 citing papers in PubMed, 166 citations in OpenAlex.

  1. Ancient origins of alkaloid biosynthesis in medicinal clubmosses.bioRxiv : the preprint server for biology · 2026
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  9. Functional Annotation from Structural Homology.Methods in molecular biology (Clifton, N.J.) · 2022
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  13. Review
  14. Early Steps in the Biosynthetic Pathway of Rishirilide B.Molecules (Basel, Switzerland) · 2020
    Article
  15. Article
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  17. How a cofactor-free protein environment lowers the barrier to OThe Journal of biological chemistry · 2019
    Article
  18. Review
  19. Article
  20. Article

6 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

9 authors at 1 institution in 1 country.

Giuliano SciaraDipartimento di Scienze Biochimiche and CNR, Centro di Studi sulla Biologia Molecolare, Università di Roma 'La Sapienza', Piazzale A.Moro, 5, 00185 Roma, Italy.
Steven G Kendrew
Adriana E Miele
Neil G Marsh
Luca Federici
Francesco Malatesta
Giuliana Schimperna
Carmelinda Savino
Beatrice Vallone
Sapienza University of Rome · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ActVA-Orf6 monooxygenase from Streptomyces coelicolor that catalyses the oxidation of an aromatic intermediate of the actinorhodin biosynthetic pathway is a member of a class of small monooxygenases that carry out oxygenation without the assistance of any of the prosthetic groups, metal ions or cofactors normally associated with activation of molecular oxygen. The overall structure is a ferredoxin-like fold with a novel dimeric assembly, indicating that the widely represented ferredoxin fold may sustain yet another functionality. The resolution (1.3 A) of the enzyme structure and its complex with substrate and product analogues allows us to visualize the mechanism of binding and activation of the substrate for attack by molecular oxygen, and utilization of two gates for the reaction components including a proton gate and an O(2)/H(2)O gate with a putative protein channel. This is the first crystal structure of an enzyme involved in the tailoring of a type II aromatic polyketide and illustrates some of the enzyme-substrate recognition features that may apply to a range of other enzymes involved in modifying a polyketide core structure.

Indexed as

Protein Structure, TertiaryAmino Acid SequenceAnthraquinonesAnti-Bacterial AgentsBenzoisochromanequinonesBinding SitesCrystallography, X-RayMixed Function OxygenasesModels, MolecularMolecular Sequence DataMolecular StructureOxygenProtein FoldingSequence AlignmentStreptomycesactinorhodinAnthraquinonesAnti-Bacterial AgentsBenzoisochromanequinonesMixed Function OxygenasesOxygen

Identifiers

PMID12514126
PMCPMC140106
OpenAlexW2095372770

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.