Evidence map›Paper›PMID 11032794›Full record

ArticleThe EMBO journal2000

X-ray crystal structure of rabbit N-acetylglucosaminyltransferase I: catalytic mechanism and a new protein superfamily.

U M Unligil, S Zhou, S Yuwaraj, M Sarkar, H Schachter, J M Rini

Abstract read
In one paragraph

Article in The EMBO journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
–field-weighted citation impact
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

68 citing papers in PubMed.

  1. Article
  2. Iterative Bump-and-Hole Engineering Creates a Bioorthogonal Reporter forJournal of the American Chemical Society · 2026
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  3. Iterative Bump-and-hole engineering creates a bioorthogonal reporter forbioRxiv : the preprint server for biology · 2026
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  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Structures of the mannose-6-phosphate pathway enzyme, GlcNAc-1-phosphotransferase.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  10. Article
  11. Structure-based design of UDP-GlcNAc analogs as candidate GnT-V inhibitors.Biochimica et biophysica acta. General subjects · 2022
    Article
  12. Towards understanding the extensive diversity of protein N-glycan structures in eukaryotes.Biological reviews of the Cambridge Philosophical Society · 2022
    Review
  13. Article
  14. Review
  15. 3D Structure and Function of Glycosyltransferases Involved inInternational journal of molecular sciences · 2020
    Review
  16. Molecular & cellular proteomics : MCP · 2019
    Article
  17. Article
  18. Article
  19. HumanProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  20. Article

8 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

6 authors.

U M UnligilDepartment of Medical Genetics and Microbiology, University of Toronto, Toronto, Ontario M5S 1A8, Canada.
S Zhou
S Yuwaraj
M Sarkar
H Schachter
J M Rini

Funding

ZINC FINGER-DNA COMPLEXP41RR001646 · NCRR · CORNELL UNIVERSITY ITHACA · PI THORNE, ROBERT E. · 1985 to 2011
$23.8M
NCRR NIH HHS P41 RR001646NCRR NIH HHS RR-01646
6 · The paper itself

Abstract

N:-acetylglucosaminyltransferase I (GnT I) serves as the gateway from oligomannose to hybrid and complex N:-glycans and plays a critical role in mammalian development and possibly all metazoans. We have determined the X-ray crystal structure of the catalytic fragment of GnT I in the absence and presence of bound UDP-GlcNAc/Mn(2+) at 1.5 and 1.8 A resolution, respectively. The structures identify residues critical for substrate binding and catalysis and provide evidence for similarity, at the mechanistic level, to the deglycosylation step of retaining beta-glycosidases. The structuring of a 13 residue loop, resulting from UDP-GlcNAc/Mn(2+) binding, provides an explanation for the ordered sequential 'Bi Bi' kinetics shown by GnT I. Analysis reveals a domain shared with Bacillus subtilis glycosyltransferase SpsA, bovine beta-1,4-galactosyl transferase 1 and Escherichia coli N:-acetylglucosamine-1-phosphate uridyltransferase. The low sequence identity, conserved fold and related functional features shown by this domain define a superfamily whose members probably share a common ancestor. Sequence analysis and protein threading show that the domain is represented in proteins from several glycosyltransferase families.

Indexed as

Evolution, MolecularAmino Acid SequenceAnimalsBinding SitesCatalysisComputational BiologyCrystallography, X-RayGlycosylationHydrogen BondingKineticsManganeseModels, MolecularMolecular Sequence DataN-AcetylglucosaminyltransferasesProtein Structure, SecondaryProtein Structure, Tertiaryalpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase IManganeseN-AcetylglucosaminyltransferasesRecombinant ProteinsUridine Diphosphate N-Acetylglucosamine

Identifiers

PMID11032794
PMCPMC314010

What OpenQuestion holds

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Registered trials

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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.