Modulation of glucan-enzyme interactions by domain V in GTF-SI from Streptococcus mutans

Manuel I. Osorio, Matías A. Zúñiga, Fernanda Mendoza, Gonzalo A. Jaña, Verónica A. Jiménez

Resultado de la investigación: Article

2 Citas (Scopus)

Resumen

Glucansucrase GTF-SI from Streptococcus mutans is a multidomain enzyme that catalyzes the synthesis of glucan polymers. Domain V locates 100 Å from the catalytic site and is required for an optimal activity. Nevertheless, the mechanism governing its functional role remains elusive. In this work, homology modeling and molecular dynamics simulations were employed to examine the effect of domain V in the structure and glucan-binding ability of GTF-SI in full and truncated enzyme models. Our results showed that domain V increases the flexibility of the α4′-loop-α4″ motif near the catalytic site resulting in a higher surface for glucan association, and modulates the orientation of a growing oligosaccharide (N=8-23) in glucan-enzyme complexes towards engaging in favorable contacts throughout the protein, whereas in the truncated model the glucan protrudes randomly from domain B towards the solvent. These results are valuable to increase understanding about the functional role of domain V in GH70 glucansucrases.

Idioma originalEnglish
Páginas (desde-hasta)74-80
Número de páginas7
PublicaciónProteins: Structure, Function and Bioinformatics
Volumen87
N.º1
DOI
EstadoPublished - 1 ene 2019

Huella dactilar

Streptococcus mutans
Glucans
alternansucrase
Modulation
Enzymes
Catalytic Domain
Molecular Dynamics Simulation
Oligosaccharides
Molecular dynamics
Polymers
Association reactions
Computer simulation
Proteins

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology

Citar esto

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abstract = "Glucansucrase GTF-SI from Streptococcus mutans is a multidomain enzyme that catalyzes the synthesis of glucan polymers. Domain V locates 100 {\AA} from the catalytic site and is required for an optimal activity. Nevertheless, the mechanism governing its functional role remains elusive. In this work, homology modeling and molecular dynamics simulations were employed to examine the effect of domain V in the structure and glucan-binding ability of GTF-SI in full and truncated enzyme models. Our results showed that domain V increases the flexibility of the α4′-loop-α4″ motif near the catalytic site resulting in a higher surface for glucan association, and modulates the orientation of a growing oligosaccharide (N=8-23) in glucan-enzyme complexes towards engaging in favorable contacts throughout the protein, whereas in the truncated model the glucan protrudes randomly from domain B towards the solvent. These results are valuable to increase understanding about the functional role of domain V in GH70 glucansucrases.",
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Modulation of glucan-enzyme interactions by domain V in GTF-SI from Streptococcus mutans. / Osorio, Manuel I.; Zúñiga, Matías A.; Mendoza, Fernanda; Jaña, Gonzalo A.; Jiménez, Verónica A.

En: Proteins: Structure, Function and Bioinformatics, Vol. 87, N.º 1, 01.01.2019, p. 74-80.

Resultado de la investigación: Article

TY - JOUR

T1 - Modulation of glucan-enzyme interactions by domain V in GTF-SI from Streptococcus mutans

AU - Osorio, Manuel I.

AU - Zúñiga, Matías A.

AU - Mendoza, Fernanda

AU - Jaña, Gonzalo A.

AU - Jiménez, Verónica A.

PY - 2019/1/1

Y1 - 2019/1/1

N2 - Glucansucrase GTF-SI from Streptococcus mutans is a multidomain enzyme that catalyzes the synthesis of glucan polymers. Domain V locates 100 Å from the catalytic site and is required for an optimal activity. Nevertheless, the mechanism governing its functional role remains elusive. In this work, homology modeling and molecular dynamics simulations were employed to examine the effect of domain V in the structure and glucan-binding ability of GTF-SI in full and truncated enzyme models. Our results showed that domain V increases the flexibility of the α4′-loop-α4″ motif near the catalytic site resulting in a higher surface for glucan association, and modulates the orientation of a growing oligosaccharide (N=8-23) in glucan-enzyme complexes towards engaging in favorable contacts throughout the protein, whereas in the truncated model the glucan protrudes randomly from domain B towards the solvent. These results are valuable to increase understanding about the functional role of domain V in GH70 glucansucrases.

AB - Glucansucrase GTF-SI from Streptococcus mutans is a multidomain enzyme that catalyzes the synthesis of glucan polymers. Domain V locates 100 Å from the catalytic site and is required for an optimal activity. Nevertheless, the mechanism governing its functional role remains elusive. In this work, homology modeling and molecular dynamics simulations were employed to examine the effect of domain V in the structure and glucan-binding ability of GTF-SI in full and truncated enzyme models. Our results showed that domain V increases the flexibility of the α4′-loop-α4″ motif near the catalytic site resulting in a higher surface for glucan association, and modulates the orientation of a growing oligosaccharide (N=8-23) in glucan-enzyme complexes towards engaging in favorable contacts throughout the protein, whereas in the truncated model the glucan protrudes randomly from domain B towards the solvent. These results are valuable to increase understanding about the functional role of domain V in GH70 glucansucrases.

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