Evidence map›Paper›PMID 27032335›Full record

ArticleScientific reports2016

Molecular characterization of a family 5 glycoside hydrolase suggests an induced-fit enzymatic mechanism.

Marcelo V Liberato, Rodrigo L Silveira, Érica T Prates, Evandro A de Araujo, Vanessa O A Pellegrini, Cesar M Camilo, Marco A Kadowaki, Mario de O Neto, Alexander Popov, Munir S Skaf and 1 more

Erratum issuedOpen access · goldAbstract readVideo-Audio Media
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

18 citing papers in PubMed, 39 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors at 2 institutions in 2 countries.

Marcelo V LiberatoSão Carlos Institute of Physics, University of São Paulo, São Carlos 13566-590 São Paulo, Brazil.
Rodrigo L SilveiraInstitute of Chemistry, University of Campinas, Campinas 13084-862, São Paulo, Brazil.
Érica T PratesInstitute of Chemistry, University of Campinas, Campinas 13084-862, São Paulo, Brazil.
Evandro A de AraujoSão Carlos Institute of Physics, University of São Paulo, São Carlos 13566-590 São Paulo, Brazil.
Vanessa O A PellegriniSão Carlos Institute of Physics, University of São Paulo, São Carlos 13566-590 São Paulo, Brazil.
Cesar M CamiloSão Carlos Institute of Physics, University of São Paulo, São Carlos 13566-590 São Paulo, Brazil.
Marco A KadowakiSão Carlos Institute of Physics, University of São Paulo, São Carlos 13566-590 São Paulo, Brazil.
Mario de O NetoInstitute of Bioscience, State University of São Paulo, Botucatu 18618-970, São Paulo, Brazil.
Alexander PopovEuropean Synchrotron Radiation Facility, Grenoble CS40220, France.
Munir S SkafInstitute of Chemistry, University of Campinas, Campinas 13084-862, São Paulo, Brazil.
Igor PolikarpovSão Carlos Institute of Physics, University of São Paulo, São Carlos 13566-590 São Paulo, Brazil.
Universidade Estadual de Campinas (UNICAMP) · BREuropean Synchrotron Radiation Facility · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycoside hydrolases (GHs) play fundamental roles in the decomposition of lignocellulosic biomaterials. Here, we report the full-length structure of a cellulase from Bacillus licheniformis (BlCel5B), a member of the GH5 subfamily 4 that is entirely dependent on its two ancillary modules (Ig-like module and CBM46) for catalytic activity. Using X-ray crystallography, small-angle X-ray scattering and molecular dynamics simulations, we propose that the C-terminal CBM46 caps the distal N-terminal catalytic domain (CD) to establish a fully functional active site via a combination of large-scale multidomain conformational selection and induced-fit mechanisms. The Ig-like module is pivoting the packing and unpacking motions of CBM46 relative to CD in the assembly of the binding subsite. This is the first example of a multidomain GH relying on large amplitude motions of the CBM46 for assembly of the catalytically competent form of the enzyme.

Indexed as

Amino Acid SequenceBacillus licheniformisBacterial ProteinsBinding SitesCatalytic DomainCelluloseConsensus SequenceCrystallography, X-RayModels, MolecularMolecular Dynamics SimulationMotionMutagenesis, Site-DirectedPhylogenyProtein ConformationProtein DomainsRecombinant ProteinsBacterial ProteinscellotetraoseCelluloseRecombinant ProteinsTetroses

Identifiers

PMID27032335
PMCPMC4817029
OpenAlexW2322888619

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.