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A computational approach to structural properties of glycoside hydrolase family 4 from bacteria

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Craciun D., Vlad-Oros B., Filimon N., Ostafe V., Isvoran A.

Acta Biochimica Polonica

2013

tom 60

nr 4

Structural bioinformatics approaches applied to the alpha- and beta-glycosidases from the GH4 enzyme family reveal that, despite low sequence identity, these enzymes possess quite similar global structural characteristics reflecting a common reaction mechanism. Locally, there are a few distinctive structural characteristics of GH4 alpha- and beta-glycosidases, namely, surface cavities with different geometric characteristics and two regions with highly dissimilar structural organizations and distinct physicochemical properties in the alpha- and beta-glucosidases from Thermotoga maritima. We suggest that these structurally dissimilar regions may be involved in specific protein-protein interactions and this hypothesis is sustained by the predicted distinct functional partners of the investigated proteins. Also, we predict that alpha- and beta-glycosidases from the GH4 enzyme family interact with difenoconazole, a fungicide, but there are different features of these interactions especially concerning the identified structurally distinct regions of the investigated proteins.

Ograniczanie wyników

1 Acta Biochimica Polonica

1 Craciun D.

1 Filimon N.

1 Isvoran A.

1 Ostafe V.

1 Vlad-Oros B.

1 2013

Wyniki wyszukiwania

A computational approach to structural properties of glycoside hydrolase family 4 from bacteria