title: A computational approach to structural properties of glycoside hydrolase family 4 from bacteria.
abstract: 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.
authors: West University of Timisoara, Teacher Training Department, Timisoara, Romania.
authors: Dana
authors: D
authors: Craciun
authors: West University of Timisoara, Department of Biology and Chemistry, Timisoara, Romania; Laboratory of Advanced Researches in Environmental Protection, Timisoara, Romania and University "Al. I. Cuza" from Lasi, Lasi, Romania (temporally affiliated).
authors: Beatrice
authors: B
authors: Vlad-Oros
authors: West University of Timisoara, Department of Biology and Chemistry, Timisoara, Romania and Laboratory of Advanced Researches in Environmental Protection, Timisoara, Romania.
authors: Nicoleta
authors: N
authors: Filimon
authors: West University of Timisoara, Department of Biology and Chemistry, Timisoara, Romania and Laboratory of Advanced Researches in Environmental Protection, Timisoara, Romania.
authors: Vasile
authors: V
authors: Ostafe
authors: West University of Timisoara, Department of Biology and Chemistry, Timisoara, Romania and Laboratory of Advanced Researches in Environmental Protection, Timisoara, Romania.
authors: Adriana
authors: A
authors: Isvoran
mesh_terms: D000595:Amino Acid Sequence; D019295:Computational Biology; D004148:Dioxolanes / Q000737:chemistry / Q000627:therapeutic use; D006026:Glycoside Hydrolases / Q000737:chemistry* / Q000378:metabolism; D006027:Glycosides / Q000737:chemistry; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D020124:Thermotoga maritima / Q000201:enzymology*; D014230:Triazoles / Q000737:chemistry / Q000627:therapeutic use
chemical_list: D004148:Dioxolanes; D006027:Glycosides; D014230:Triazoles; C115058:difenoconazole; D006026:Glycoside Hydrolases