Evidence map›Paper›PMID 19097997›Full record

ArticleThe Journal of biological chemistry2009

Molecular mechanisms of yeast cell wall glucan remodeling.

Ramon Hurtado-Guerrero, Alexander W Schüttelkopf, Isabelle Mouyna, Adel F M Ibrahim, Sharon Shepherd, Thierry Fontaine, Jean-Paul Latgé, Daan M F van Aalten

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

31 citing papers in PubMed, 88 citations in OpenAlex.

  1. Article
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  7. Article
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  10. Review
  11. Cell wall polysaccharides: before and after autolysis of brewer's yeast.World journal of microbiology & biotechnology · 2018
    Review
  12. Article
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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

8 authors at 2 institutions in 2 countries.

Ramon Hurtado-GuerreroDivision of Biological Chemistry and Drug Discovery, College of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, United Kingdom. R.Hurtadoguerrero@dundee.ac.uk
Alexander W Schüttelkopf
Isabelle Mouyna
Adel F M Ibrahim
Sharon Shepherd
Thierry Fontaine
Jean-Paul Latgé
Daan M F van Aalten
University of Dundee · GBInstitut Pasteur · FR

Funding

Wellcome Trust 087590
6 · The paper itself

Abstract

Yeast cell wall remodeling is controlled by the equilibrium between glycoside hydrolases, glycosyltransferases, and transglycosylases. Family 72 glycoside hydrolases (GH72) are ubiquitous in fungal organisms and are known to possess significant transglycosylase activity, producing elongated beta(1-3) glucan chains. However, the molecular mechanisms that control the balance between hydrolysis and transglycosylation in these enzymes are not understood. Here we present the first crystal structure of a glucan transglycosylase, Saccharomyces cerevisiae Gas2 (ScGas2), revealing a multidomain fold, with a (betaalpha)(8) catalytic core and a separate glucan binding domain with an elongated, conserved glucan binding groove. Structures of ScGas2 complexes with different beta-glucan substrate/product oligosaccharides provide "snapshots" of substrate binding and hydrolysis/transglycosylation giving the first insights into the mechanisms these enzymes employ to drive beta(1-3) glucan elongation. Together with mutagenesis and analysis of reaction products, the structures suggest a "base occlusion" mechanism through which these enzymes protect the covalent protein-enzyme intermediate from a water nucleophile, thus controlling the balance between hydrolysis and transglycosylation and driving the elongation of beta(1-3) glucan chains in the yeast cell wall.

Indexed as

Protein FoldingCell WallCrystallography, X-RayGlucan Endo-1,3-beta-D-GlucosidaseGlucansProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae Proteins1,3-beta-glucanosyltransferaseGlucan Endo-1,3-beta-D-GlucosidaseGlucansSaccharomyces cerevisiae Proteins

Identifiers

PMID19097997
PMCPMC2659204
OpenAlexW2074723587

What OpenQuestion holds

Textmetadata
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.