Evidence map›Paper›PMID 20081828›Full record

ArticleNature chemical biology2010

Mechanistic insights into a Ca2+-dependent family of alpha-mannosidases in a human gut symbiont.

Yanping Zhu, Michael D L Suits, Andrew J Thompson, Sambhaji Chavan, Zoran Dinev, Claire Dumon, Nicola Smith, Kelley W Moremen, Yong Xiang, Aloysius Siriwardena and 3 more

Open access · greenAbstract read
In one paragraph

Article in Nature chemical biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
9.0field-weighted citation impact, top 2% 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

66 citing papers in PubMed, 141 citations in OpenAlex.

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  13. Inducible CRISPR-targeted "knockdown" of human gutProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
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  19. PlantProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  20. Article

6 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

13 authors at 7 institutions in 4 countries.

Yanping ZhuInstitute for Cell and Molecular Biosciences, The Medical School, Newcastle University, Framlington Place, Newcastle upon Tyne, UK.
Michael D L Suits
Andrew J Thompson
Sambhaji Chavan
Zoran Dinev
Claire Dumon
Nicola Smith
Kelley W Moremen
Yong Xiang
Aloysius Siriwardena
Spencer J Williams
Harry J Gilbert
Gideon J Davies
Newcastle University · GBUniversity of York · GBThe University of Melbourne · AUUniversity of Georgia · USCentre National de la Recherche Scientifique · FRUniversité de Picardie Jules Verne · FRUniversité Toulouse III - Paul Sabatier · FR

Funding

ZINC DEFICIENCY &PROTEIN EXPRESSION IN RAT OLFACTORY BULBSP41RR005351 · NCRR · UNIVERSITY OF GEORGIA (UGA) · PI MOREMEN, KELLEY W. · 1989 to 2011
$18.4M
TR&D3. Approaches to Proteoglycan Function at Biochemical and Cellular LevelsP41GM103390 · NIGMS · UNIVERSITY OF GEORGIA · PI LIVE, DAVID H · 2012 to 2019
$14.5M
Mannosidases in Glycoprotein Biosynthesis &CatabolismR01GM047533 · NIGMS · UNIVERSITY OF GEORGIA (UGA) · PI MOREMEN, KELLEY W. · 1992 to 2008
$2.6M
Mannosidase inhibitors as therapeutics for glycoprotein misfolding diseasesR01DK075322 · NIDDK · UNIVERSITY OF GEORGIA · PI MOREMEN, KELLEY W. · 2006 to 2010
$2.6M
Biotechnology and Biological Sciences Research Council BB/E000568/1Biotechnology and Biological Sciences Research Council BB/G016127/1NCRR NIH HHS P41 RR005351NCRR NIH HHS RR005351NIDDK NIH HHS DK075322NIDDK NIH HHS R01 DK075322NIGMS NIH HHS GM047533NIGMS NIH HHS P41 GM103390NIGMS NIH HHS R01 GM047533
6 · The paper itself

Abstract

Colonic bacteria, exemplified by Bacteroides thetaiotaomicron, play a key role in maintaining human health by harnessing large families of glycoside hydrolases (GHs) to exploit dietary polysaccharides and host glycans as nutrients. Such GH family expansion is exemplified by the 23 family GH92 glycosidases encoded by the B. thetaiotaomicron genome. Here we show that these are alpha-mannosidases that act via a single displacement mechanism to utilize host N-glycans. The three-dimensional structure of two GH92 mannosidases defines a family of two-domain proteins in which the catalytic center is located at the domain interface, providing acid (glutamate) and base (aspartate) assistance to hydrolysis in a Ca(2+)-dependent manner. The three-dimensional structures of the GH92s in complex with inhibitors provide insight into the specificity, mechanism and conformational itinerary of catalysis. Ca(2+) plays a key catalytic role in helping distort the mannoside away from its ground-state (4)C(1) chair conformation toward the transition state.

Indexed as

Symbiosisalpha-MannosidaseBacteroidesCalciumCatalytic DomainCrystallography, X-RayHumansIntestinesModels, MolecularPolysaccharidesProtein Structure, TertiarySubstrate Specificityalpha-MannosidaseCalciumPolysaccharides

Identifiers

PMID20081828
PMCPMC3942423
OpenAlexW2038048096

What OpenQuestion holds

Textmetadata
LicenceTDM
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.