Evidence map›Paper›PMID 20097205›Full record

ArticleJournal of molecular biology2010

Structural basis of substrate binding in WsaF, a rhamnosyltransferase from Geobacillus stearothermophilus.

Kerstin Steiner, Gregor Hagelueken, Paul Messner, Christina Schäffer, James H Naismith

Abstract read
In one paragraph

Article in Journal of molecular biology, 2010. 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. Review
  3. Article
  4. Emerging facets of prokaryotic glycosylation.FEMS microbiology reviews · 2017
    Review
  5. Article
  6. Review
  7. Bacterial cell-envelope glycoconjugates.Advances in carbohydrate chemistry and biochemistry · 2013
    Review
  8. Article
  9. Article
  10. Review
  11. The s-layer glycome-adding to the sugar coat of bacteria.International journal of microbiology · 2011
    Article
  12. Article
  13. Article
  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

5 authors.

Kerstin SteinerCentre for Biomolecular Sciences, University of St. Andrews, North Haugh, St. Andrews, Fife KY16 9ST, UK.
Gregor Hagelueken
Paul Messner
Christina Schäffer
James H Naismith

Funding

Austrian Science Fund FWF J 2746Austrian Science Fund FWF P 19047Austrian Science Fund FWF P 20745Austrian Science Fund FWF P 21954Wellcome Trust 081862
6 · The paper itself

Abstract

Carbohydrate polymers are medically and industrially important. The S-layer of many Gram-positive organisms comprises protein and carbohydrate polymers and forms an almost paracrystalline array on the cell surface. Not only is this array important for the bacteria but it has potential application in the manufacture of commercially important polysaccharides and glycoconjugates as well. The S-layer glycoprotein glycan from Geobacillus stearothermophilus NRS 2004/3a is mainly composed of repeating units of three rhamnose sugars linked by alpha-1,3-, alpha-1,2-, and beta-1,2-linkages. The formation of the beta-1,2-linkage is catalysed by the enzyme WsaF. The rational use of this system is hampered by the fact that WsaF and other enzymes in the pathway share very little homology to other enzymes. We report the structural and biochemical characterisation of WsaF, the first such rhamnosyltransferase to be characterised. Structural work was aided by the surface entropy reduction method. The enzyme has two domains, the N-terminal domain, which binds the acceptor (the growing rhamnan chain), and the C-terminal domain, which binds the substrate (dTDP-beta-l-rhamnose). The structure of WsaF bound to dTDP and dTDP-beta-l-rhamnose coupled to biochemical analysis identifies the residues that underlie catalysis and substrate recognition. We have constructed and tested by site-directed mutagenesis a model for acceptor recognition.

Indexed as

Amino Acid SubstitutionBinding SitesCatalytic DomainDeoxy SugarsGeobacillus stearothermophilusHexosyltransferasesMannansModels, MolecularMutagenesis, Site-DirectedMutant ProteinsNucleoside Diphosphate SugarsProtein BindingProtein Structure, TertiaryThymine NucleotidesDeoxy SugarsHexosyltransferasesMannansMutant ProteinsNucleoside Diphosphate Sugarsrhamnanthymidine diphosphate rhamnoseThymine Nucleotides

Identifiers

PMID20097205
PMCPMC3898925

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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.