Evidence map›Paper›PMID 18505738›Full record

ArticleProtein science : a publication of the Protein Society2008

Crystal structure and mutagenic analysis of GDOsp, a gentisate 1,2-dioxygenase from Silicibacter pomeroyi.

Jia Chen, Wei Li, Mingzhu Wang, Guangyu Zhu, Dongqi Liu, Fei Sun, Ning Hao, Xuemei Li, Zihe Rao, Xuejun C Zhang

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.3field-weighted citation impact, top 19% of its field
1 · What the graph read from it

What it found

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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

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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

20 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. Characterization of the substrate specificity and regioselectivity of ring-cleavage of Pseudomonas putida DLL-E4 hydroquinone 1,2-dioxygenase (PnpC1C2).Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025
    Article
  3. Review
  4. Proton Transfer via Arginine with Suppressed pThe journal of physical chemistry. B · 2024
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  8. Article
  9. Substrate promiscuity and active site differences in gentisate 1,2-dioxygenases: electron paramagnetic resonance study.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2019
    Article
  10. A Biomimetic System for Studying Salicylate Dioxygenase.ACS symposium series. American Chemical Society · 2019
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  15. Article
  16. Structure of the 2,4'-dihydroxyacetophenone dioxygenase from Alcaligenes sp. 4HAP.Acta crystallographica. Section D, Biological crystallography · 2014
    Article
  17. Review
  18. Article
  19. Crystallization and preliminary X-ray crystallographic analysis of hydroquinone dioxygenase from Sphingomonas sp. TTNP3.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012
    Article
  20. Ring-cleaving dioxygenases with a cupin fold.Applied and environmental microbiology · 2012
    Review
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 6 institutions in 2 countries.

Jia ChenNational Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, People's Republic of China.
Wei Li
Mingzhu Wang
Guangyu Zhu
Dongqi Liu
Fei Sun
Ning Hao
Xuemei Li
Zihe Rao
Xuejun C Zhang
Chinese Academy of Sciences · CNInstitute of Biophysics · CNHuazhong University of Science and Technology · CNNankai University · CNOklahoma Medical Research Foundation · USWuhan Institute of Virology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dioxygenases catalyze dioxygen incorporation into various organic compounds and play a key role in the complex degradation pathway of mono- and polycyclic aromatic and hetero-aromatic compounds. Here we report the crystal structure of gentisate 1,2-dioxygenase from Silicibacter pomeroyi (GDOsp) at a 2.8 A resolution. The enzyme possessed a conserved three-dimensional structure of the bicupin family, forming a homotetramerization. However, each subunit of GDOsp unusually contained two ferrous centers that were located in its two homologous cupin domains, respectively. Further mutagenic analysis indicated that the enzyme activity of GDOsp depends on the microenvironment in both metal-binding sites. Moreover, homologous structural comparison and functional study on GDOsp variants unveiled a group of functionally essential residues and suggested that the active site of the enzyme is located in the amino-terminal domain, but could be influenced by changes in the carboxyl domain. Therefore, GDOsp may provide a working model for studying long-distance communication within a protein (or its complex).

Indexed as

Amino Acid SequenceBacterial ProteinsCatalytic DomainCircular DichroismCrystallography, X-RayDimerizationDioxygenasesMolecular Sequence DataMolecular StructureMutagenesisMutationProtein BindingProtein FoldingProtein Structure, TertiaryRhodobacteraceaeSequence Homology, Amino AcidBacterial ProteinsDioxygenasesgentisate 1,2-dioxygenase

Identifiers

PMID18505738
PMCPMC2492823
OpenAlexW2127874990

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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.