Evidence map›Paper›PMID 23959893›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Glycosylated linkers in multimodular lignocellulose-degrading enzymes dynamically bind to cellulose.

Christina M Payne, Michael G Resch, Liqun Chen, Michael F Crowley, Michael E Himmel, Larry E Taylor, Mats Sandgren, Jerry Ståhlberg, Ingeborg Stals, Zhongping Tan and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
14.1field-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

64 citing papers in PubMed, 188 citations in OpenAlex.

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  7. Engineering cellulases for conversion of lignocellulosic biomass.Protein engineering, design & selection : PEDS · 2023
    Review
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4 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

11 authors at 5 institutions in 3 countries.

Christina M PayneBiosciences Center and National Bioenergy Center, National Renewable Energy Laboratory, Golden, CO 80401, USA
Michael G Resch
Liqun Chen
Michael F Crowley
Michael E Himmel
Larry E Taylor
Mats Sandgren
Jerry Ståhlberg
Ingeborg Stals
Zhongping Tan
Gregg T Beckham
Swedish University of Agricultural Sciences · SEUniversity of Colorado Boulder · USNational Renewable Energy Laboratory · USUniversity College Ghent · BEUniversity of Kentucky · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plant cell-wall polysaccharides represent a vast source of food in nature. To depolymerize polysaccharides to soluble sugars, many organisms use multifunctional enzyme mixtures consisting of glycoside hydrolases, lytic polysaccharide mono-oxygenases, polysaccharide lyases, and carbohydrate esterases, as well as accessory, redox-active enzymes for lignin depolymerization. Many of these enzymes that degrade lignocellulose are multimodular with carbohydrate-binding modules (CBMs) and catalytic domains connected by flexible, glycosylated linkers. These linkers have long been thought to simply serve as a tether between structured domains or to act in an inchworm-like fashion during catalytic action. To examine linker function, we performed molecular dynamics (MD) simulations of the Trichoderma reesei Family 6 and Family 7 cellobiohydrolases (TrCel6A and TrCel7A, respectively) bound to cellulose. During these simulations, the glycosylated linkers bind directly to cellulose, suggesting a previously unknown role in enzyme action. The prediction from the MD simulations was examined experimentally by measuring the binding affinity of the Cel7A CBM and the natively glycosylated Cel7A CBM-linker. On crystalline cellulose, the glycosylated linker enhances the binding affinity over the CBM alone by an order of magnitude. The MD simulations before and after binding of the linker also suggest that the bound linker may affect enzyme action due to significant damping in the enzyme fluctuations. Together, these results suggest that glycosylated linkers in carbohydrate-active enzymes, which are intrinsically disordered proteins in solution, aid in dynamic binding during the enzymatic deconstruction of plant cell walls.

Indexed as

Binding, CompetitiveBinding SitesBiocatalysisCatalytic DomainCelluloseCellulose 1,4-beta-CellobiosidaseFungal ProteinsGlycosylationHydrolysisLigninMass SpectrometryModels, MolecularMolecular Dynamics SimulationProtein BindingTrichodermaCelluloseCellulose 1,4-beta-CellobiosidaseFungal ProteinsLigninlignocellulosebiofuelscarbohydrate recognitioncellulasepost-translational modification

Identifiers

PMID23959893
PMCPMC3767562
OpenAlexW2049470922

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.