Evidence map›Paper›PMID 9218781›Full record

ArticleThe EMBO journal1997

Crystal structure of human glyoxalase I--evidence for gene duplication and 3D domain swapping.

A D Cameron, B Olin, M Ridderström, B Mannervik, T A Jones

Abstract read
In one paragraph

Article in The EMBO journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
12.1field-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

65 citing papers in PubMed, 235 citations in OpenAlex.

  1. Review
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  6. Rapid transcriptomic and physiological changes in the freshwater pennate diatom Mayamaea pseudoterrestris in response to copper exposure.DNA research : an international journal for rapid publication of reports on genes and genomes · 2022
    Article
  7. Article
  8. Review
  9. Article
  10. Glyoxalase System in the Progression of Skin Aging and Skin Malignancies.International journal of molecular sciences · 2020
    Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
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  18. Review
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  20. Article

5 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

5 authors at 1 institution in 1 country.

A D CameronDepartment of Molecular Biology, Uppsala University, Biomedical Center, Sweden.
B Olin
M Ridderström
B Mannervik
T A Jones
Uppsala University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The zinc metalloenzyme glyoxalase I catalyses the glutathione-dependent inactivation of toxic methylglyoxal. The structure of the dimeric human enzyme in complex with S-benzyl-glutathione has been determined by multiple isomorphous replacement (MIR) and refined at 2.2 A resolution. Each monomer consists of two domains. Despite only low sequence homology between them, these domains are structurally equivalent and appear to have arisen by a gene duplication. On the other hand, there is no structural homology to the 'glutathione binding domain' found in other glutathione-linked proteins. 3D domain swapping of the N- and C-terminal domains has resulted in the active site being situated in the dimer interface, with the inhibitor and essential zinc ion interacting with side chains from both subunits. Two structurally equivalent residues from each domain contribute to a square pyramidal coordination of the zinc ion, rarely seen in zinc enzymes. Comparison of glyoxalase I with other known structures shows the enzyme to belong to a new structural family which includes the Fe2+-dependent dihydroxybiphenyl dioxygenase and the bleomycin resistance protein. This structural family appears to allow members to form with or without domain swapping.

Indexed as

Multigene FamilyProtein Structure, SecondaryAmino Acid SequenceBinding SitesCrystallography, X-RayGlutathioneHumansImage Processing, Computer-AssistedLactoylglutathione LyaseModels, MolecularMolecular Sequence DataRecombinant Fusion ProteinsSequence Homology, Amino AcidZincGlutathioneLactoylglutathione LyaseRecombinant Fusion ProteinsZinc

Identifiers

PMID9218781
PMCPMC1169964
OpenAlexW2157331625

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.