Evidence map›Paper›PMID 28608671›Full record

ArticleBiochemistry2017

Conformational Control of UDP-Galactopyranose Mutase Inhibition.

Kittikhun Wangkanont, Valerie J Winton, Katrina T Forest, Laura L Kiessling

Abstract readComparative Study
PubMed Full text at PMC Publisher
In one paragraph

Article in Biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. 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

4 authors.

Kittikhun WangkanontDepartment of Chemistry, ‡Department of Biochemistry, and §Department of Bacteriology, University of Wisconsin-Madison , Madison, Wisconsin 53706, United States.ORCID 0000-0002-7190-2955
Valerie J WintonDepartment of Chemistry, ‡Department of Biochemistry, and §Department of Bacteriology, University of Wisconsin-Madison , Madison, Wisconsin 53706, United States.
Katrina T ForestDepartment of Chemistry, ‡Department of Biochemistry, and §Department of Bacteriology, University of Wisconsin-Madison , Madison, Wisconsin 53706, United States.
Laura L KiesslingDepartment of Chemistry, ‡Department of Biochemistry, and §Department of Bacteriology, University of Wisconsin-Madison , Madison, Wisconsin 53706, United States.ORCID 0000-0001-6829-1500

Funding

X-RAY STRUCTURE OF RIFM PROTEIN FROM THE BIOSYNTHESIS PATHWAY OF THE ANSAMYCIN AP41RR012408 · NCRR · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI ORVILLE, ALLEN M · 1998 to 2011
$32.2M
X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
The Chemistry and Biology of Galactofuranose-Containing GlycansR01AI126592 · NIAID · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI Laura L Kiessling · 2017 to 2026
$5.2M
Macromolecular Crystallography at the National Synchrotron Light SourceP41GM103473 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI SWEET, ROBERT M · 2012 to 2013
$4.9M
The Chemistry and Biology of Galactofuranose ResiduesR01AI063596 · NIAID · UNIVERSITY OF WISCONSIN-MADISON · PI KIESSLING, LAURA L · 2005 to 2014
$3.0M
NCRR NIH HHS P41 RR012408NIAID NIH HHS R01 AI063596NIAID NIH HHS R01 AI126592NIGMS NIH HHS P41 GM103393NIGMS NIH HHS P41 GM103473
6 · The paper itself

Abstract

UDP-galactopyranose mutase (Glf or UGM) catalyzes the formation of uridine 5'-diphosphate-α-d-galactofuranose (UDP-Galf) from UDP-galactopyranose (UDP-Galp). The enzyme is required for the production of Galf-containing glycans. UGM is absent in mammals, but members of the Corynebacterineae suborder require UGM for cell envelope biosynthesis. The need for UGM in some pathogens has prompted the search for inhibitors that could serve as antibiotic leads. Optimizing inhibitor potency, however, has been challenging. The UGM from Klebsiella pneumoniae (KpUGM), which is not required for viability, is more effectively impeded by small-molecule inhibitors than are essential UGMs from species such as Mycobacterium tuberculosis or Corynebacterium diphtheriae. Why KpUGM is more susceptible to inhibition than other orthologs is not clear. One potential source of difference is UGM ortholog conformation. We previously determined a structure of CdUGM bound to a triazolothiadiazine inhibitor in the open form, but it was unclear whether the small-molecule inhibitor bound this form or to the closed form. By varying the terminal tag (CdUGM-His

Indexed as

Models, MolecularAnti-Bacterial AgentsBacterial ProteinsBinding SitesCatalytic DomainCorynebacterium diphtheriaeCrystallography, X-RayEnzyme InhibitorsIntramolecular TransferasesKineticsKlebsiella pneumoniaeLigandsMolecular ConformationMutagenesis, Site-DirectedMutationMycobacterium tuberculosisAnti-Bacterial AgentsBacterial ProteinsEnzyme InhibitorsIntramolecular TransferasesLigandsRecombinant Fusion ProteinsUDP-galactopyranose mutase

Identifiers

PMID28608671
PMCPMC5739916

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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.