Evidence map›Paper›PMID 23430743›Full record

ArticleThe Journal of biological chemistry2013

Three-dimensional structure of Saccharomyces invertase: role of a non-catalytic domain in oligomerization and substrate specificity.

M Angela Sainz-Polo, Mercedes Ramírez-Escudero, Alvaro Lafraya, Beatriz González, Julia Marín-Navarro, Julio Polaina, Julia Sanz-Aparicio

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. 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
6.9field-weighted citation impact, top 2% 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, 106 citations in OpenAlex.

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  13. Insights into the Structure of the Highly Glycosylated Ffase fromInternational journal of molecular sciences · 2022
    Article
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  20. UniqueJournal of biological engineering · 2019
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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

7 authors at 2 institutions in 1 country.

M Angela Sainz-PoloDepartamento de Cristalografía y Biología Estructural, Instituto de Química-Física "Rocasolano," Consejo Superior de Investigaciones Científicas (CSIC), Serrano 119, 28006 Madrid.
Mercedes Ramírez-EscuderoDepartamento de Cristalografía y Biología Estructural, Instituto de Química-Física "Rocasolano," Consejo Superior de Investigaciones Científicas (CSIC), Serrano 119, 28006 Madrid.
Alvaro LafrayaInstituto de Agroquímica y Tecnología de Alimentos, CSIC, 46980 Paterna, Valencia, Spain.
Beatriz GonzálezDepartamento de Cristalografía y Biología Estructural, Instituto de Química-Física "Rocasolano," Consejo Superior de Investigaciones Científicas (CSIC), Serrano 119, 28006 Madrid.
Julia Marín-NavarroInstituto de Agroquímica y Tecnología de Alimentos, CSIC, 46980 Paterna, Valencia, Spain.
Julio PolainaInstituto de Agroquímica y Tecnología de Alimentos, CSIC, 46980 Paterna, Valencia, Spain.
Julia Sanz-AparicioDepartamento de Cristalografía y Biología Estructural, Instituto de Química-Física "Rocasolano," Consejo Superior de Investigaciones Científicas (CSIC), Serrano 119, 28006 Madrid. Electronic address: xjulia@iqfr.csic.es.
Consejo Superior de Investigaciones Científicas · ESInstituto de Agroquímica y Tecnología de Alimentos · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Invertase is an enzyme that is widely distributed among plants and microorganisms and that catalyzes the hydrolysis of the disaccharide sucrose into glucose and fructose. Despite the important physiological role of Saccharomyces invertase (SInv) and the historical relevance of this enzyme as a model in early biochemical studies, its structure had not yet been solved. We report here the crystal structure of recombinant SInv at 3.3 Å resolution showing that the enzyme folds into the catalytic β-propeller and β-sandwich domains characteristic of GH32 enzymes. However, SInv displays an unusual quaternary structure. Monomers associate in two different kinds of dimers, which are in turn assembled into an octamer, best described as a tetramer of dimers. Dimerization plays a determinant role in substrate specificity because this assembly sets steric constraints that limit the access to the active site of oligosaccharides of more than four units. Comparative analysis of GH32 enzymes showed that formation of the SInv octamer occurs through a β-sheet extension that seems unique to this enzyme. Interaction between dimers is determined by a short amino acid sequence at the beginning of the β-sandwich domain. Our results highlight the role of the non-catalytic domain in fine-tuning substrate specificity and thus supplement our knowledge of the activity of this important family of enzymes. In turn, this gives a deeper insight into the structural features that rule modularity and protein-carbohydrate recognition.

Indexed as

Amino Acid Sequencebeta-FructofuranosidaseCarbohydratesCatalysisCatalytic DomainCloning, MolecularCrystallography, X-RayDimerizationEscherichia coliGlycoside HydrolasesKineticsModels, MolecularMolecular ConformationMolecular Sequence DataProtein ConformationProteinsbeta-FructofuranosidaseCarbohydratesGlycoside HydrolasesProteins

Identifiers

PMID23430743
PMCPMC3617277
OpenAlexW2011896456

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.