Evidence map›Paper›PMID 27856757›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Neutron structures of the Helicobacter pylori 5'-methylthioadenosine nucleosidase highlight proton sharing and protonation states.

Michael T Banco, Vidhi Mishra, Andreas Ostermann, Tobias E Schrader, Gary B Evans, Andrey Kovalevsky, Donald R Ronning

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. On the Case of the Misplaced Hydrogens.Chembiochem : a European journal of chemical biology · 2021
    Review
  7. Article
  8. Low barrier hydrogen bonds in protein structure and function.Biochimica et biophysica acta. Proteins and proteomics · 2021
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Immucillins in Infectious Diseases.ACS infectious diseases · 2018
    Review
  14. 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

7 authors.

Michael T BancoDepartment of Chemistry and Biochemistry, University of Toledo, Toledo, OH 43606.
Vidhi MishraDepartment of Chemistry and Biochemistry, University of Toledo, Toledo, OH 43606.
Andreas OstermannHeinz Maier-Leibnitz Zentrum, Technische Universität München, 85748 Garching, Germany.
Tobias E SchraderJülich Centre for Neutron Science at Heinz Maier-Leibnitz Zentrum, Forschungszentrum Jülich GmbH, 85747 Garching, Germany.
Gary B EvansFerrier Research Institute, Victoria University of Wellington, Wellington 5010, New Zealand.
Andrey KovalevskyBiology and Soft Matter Division, Oak Ridge National Laboratory, Oak Ridge, TN 37831.
Donald R RonningDepartment of Chemistry and Biochemistry, University of Toledo, Toledo, OH 43606; donald.ronning@utoledo.edu.

Funding

Understanding trehalose synthesis and utilization in mycobacteriaR01AI105084 · NIAID · UNIVERSITY OF TOLEDO · PI RONNING, DONALD R, SUCHECK, STEVEN · 2013 to 2022
$3.7M
NIAID NIH HHS R01 AI105084
6 · The paper itself

Abstract

MTAN (5'-methylthioadenosine nucleosidase) catalyzes the hydrolysis of the N-ribosidic bond of a variety of adenosine-containing metabolites. The Helicobacter pylori MTAN (HpMTAN) hydrolyzes 6-amino-6-deoxyfutalosine in the second step of the alternative menaquinone biosynthetic pathway. Substrate binding of the adenine moiety is mediated almost exclusively by hydrogen bonds, and the proposed catalytic mechanism requires multiple proton-transfer events. Of particular interest is the protonation state of residue D198, which possesses a pK

Indexed as

AdenineCatalytic DomainCrystallography, X-RayDeoxyadenosinesFormycinsHelicobacter pyloriHydrogen BondingModels, MolecularNeutronsProtein BindingProtonsPurine-Nucleoside PhosphorylasePyrrolidinesS-AdenosylhomocysteineSubstrate SpecificityThionucleosides4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin A5'-methylthioadenosine5'-methylthioadenosine phosphorylaseAdenineDeoxyadenosinesformycinFormycinsProtonsPurine-Nucleoside PhosphorylasePyrrolidinesS-AdenosylhomocysteineThionucleosidesenzyme mechanismHelicobacterneutron diffractionnucleosidaseproton transfer

Identifiers

PMID27856757
PMCPMC5137710

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.