Evidence map›Paper›PMID 20164409›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Atomic details of near-transition state conformers for enzyme phosphoryl transfer revealed by MgF-3 rather than by phosphoranes.

Nicola J Baxter, Matthew W Bowler, Tooba Alizadeh, Matthew J Cliff, Andrea M Hounslow, Bin Wu, David B Berkowitz, Nicholas H Williams, G Michael Blackburn, Jonathan P Waltho

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
–field-weighted citation impact
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

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

30 citing papers in PubMed.

  1. Article
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  3. Article
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  5. Article
  6. Article
  7. Biomolecular NMR assignments · 2019
    Article
  8. Article
  9. Article
  10. Evidence for substrate-assisted catalysis inThe Biochemical journal · 2018
    Article
  11. Article
  12. Article
  13. Article
  14. Biomolecular NMR assignments · 2017
    Article
  15. Pulmonary fluorosis: a review.Environmental science and pollution research international · 2017
    Review
  16. Article
  17. Article
  18. 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

10 authors.

Nicola J BaxterDepartment of Molecular Biology and Biotechnology, University of Sheffield, Sheffield S10 2TN, United Kingdom.
Matthew W Bowler
Tooba Alizadeh
Matthew J Cliff
Andrea M Hounslow
Bin Wu
David B Berkowitz
Nicholas H Williams
G Michael Blackburn
Jonathan P Waltho

Funding

EXTRAMURAL RES FACILITIES CONSTRC06RR016544 · NCRR · UNIVERSITY OF NEBRASKA LINCOLN · PI PAUL, PREM S · 2001 to 2001
$2.0M
NCRR NIH HHS C06 RR016544
6 · The paper itself

Abstract

Prior evidence supporting the direct observation of phosphorane intermediates in enzymatic phosphoryl transfer reactions was based on the interpretation of electron density corresponding to trigonal species bridging the donor and acceptor atoms. Close examination of the crystalline state of beta-phosphoglucomutase, the archetypal phosphorane intermediate-containing enzyme, reveals that the trigonal species is not PO-3 , but is MgF-3 (trifluoromagnesate). Although MgF-3 complexes are transition state analogues rather than phosphoryl group transfer reaction intermediates, the presence of fluorine nuclei in near-transition state conformations offers new opportunities to explore the nature of the interactions, in particular the independent measures of local electrostatic and hydrogen-bonding distributions using 19F NMR. Measurements on three beta-PGM-MgF-3 -sugar phosphate complexes show a remarkable relationship between NMR chemical shifts, primary isotope shifts, NOEs, cross hydrogen bond F...H-N scalar couplings, and the atomic positions determined from the high-resolution crystal structure of the beta-PGM-MgF--3 -G6P complex. The measurements provide independent validation of the structural and isoelectronic MgF--3 model of near-transition state conformations.

Indexed as

Catalytic DomainCrystallography, X-RayFluoridesGlucosephosphatesHydrogen BondingMagnesium CompoundsMagnetic Resonance SpectroscopyModels, MolecularMolecular ConformationMolecular StructurePhosphatesPhosphoglucomutasePhosphoranesProtein BindingProtein ConformationFluoridesGlucosephosphatesMagnesium CompoundsPhosphatesPhosphoglucomutasePhosphoranes

Identifiers

PMID20164409
PMCPMC2842025

What OpenQuestion holds

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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.