Evidence map›Paper›PMID 19218457›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

Evidence that family 35 carbohydrate binding modules display conserved specificity but divergent function.

Cedric Montanier, Alicia Lammerts van Bueren, Claire Dumon, James E Flint, Marcia A Correia, Jose A Prates, Susan J Firbank, Richard J Lewis, Gilles G Grondin, Mariana G Ghinet and 11 more

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
9.7field-weighted citation impact, top 1% 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

48 citing papers in PubMed, 122 citations in OpenAlex.

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  12. A pair of esterases from a commensal gut bacterium remove acetylations from all positions on complex β-mannans.Proceedings of the National Academy of Sciences of the United States of America · 2020
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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

21 authors at 6 institutions in 3 countries.

Cedric MontanierInstitute for Cell and Molecular Biosciences, The Medical School, Newcastle University, Newcastle upon Tyne NE2 4HH, United Kingdom.
Alicia Lammerts van Bueren
Claire Dumon
James E Flint
Marcia A Correia
Jose A Prates
Susan J Firbank
Richard J Lewis
Gilles G Grondin
Mariana G Ghinet
Tracey M Gloster
Cecile Herve
J Paul Knox
Brian G Talbot
Johan P Turkenburg
Janne Kerovuo
Ryszard Brzezinski
Carlos M G A Fontes
Gideon J Davies
Alisdair B Boraston
Harry J Gilbert
Newcastle University · GBUniversité de Sherbrooke · CAUniversity of York · GBUniversity of Leeds · GBUniversity of Victoria · CALos Alamos National Laboratory · US

Funding

Biotechnology and Biological Sciences Research Council BB/C005074/1Biotechnology and Biological Sciences Research Council BB/E014364/1Biotechnology and Biological Sciences Research Council BB/E015190/1Wellcome Trust 082572
6 · The paper itself

Abstract

Enzymes that hydrolyze complex carbohydrates play important roles in numerous biological processes that result in the maintenance of marine and terrestrial life. These enzymes often contain noncatalytic carbohydrate binding modules (CBMs) that have important substrate-targeting functions. In general, there is a tight correlation between the ligands recognized by bacterial CBMs and the substrate specificity of the appended catalytic modules. Through high-resolution structural studies, we demonstrate that the architecture of the ligand binding sites of 4 distinct family 35 CBMs (CBM35s), appended to 3 plant cell wall hydrolases and the exo-beta-D-glucosaminidase CsxA, which contributes to the detoxification and metabolism of an antibacterial fungal polysaccharide, is highly conserved and imparts specificity for glucuronic acid and/or Delta4,5-anhydrogalaturonic acid (Delta4,5-GalA). Delta4,5-GalA is released from pectin by the action of pectate lyases and as such acts as a signature molecule for plant cell wall degradation. Thus, the CBM35s appended to the 3 plant cell wall hydrolases, rather than targeting the substrates of the cognate catalytic modules, direct their appended enzymes to regions of the plant that are being actively degraded. Significantly, the CBM35 component of CsxA anchors the enzyme to the bacterial cell wall via its capacity to bind uronic acid sugars. This latter observation reveals an unusual mechanism for bacterial cell wall enzyme attachment. This report shows that the biological role of CBM35s is not dictated solely by their carbohydrate specificities but also by the context of their target ligands.

Indexed as

ActinomycetalesCarbohydrate MetabolismCarbohydratesCell AdhesionCell WallGalectin 3LigandsModels, MolecularMolecular StructureMutationProtein BindingSubstrate SpecificityThermodynamicsUronic AcidsCarbohydratesGalectin 3LigandsUronic Acids

Identifiers

PMID19218457
PMCPMC2651348
OpenAlexW2012200956

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.