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

被引：0

作者：

Craciun, Dana ^{[1
]}

Vlad-Oros, Beatrice ^{[2
,3
]}

Filimon, Nicoleta ^{[2
,3
]}

Ostafe, Vasile ^{[2
,3
]}

Isvoran, Adriana ^{[2
,3
]}

机构：

[1] West Univ Timisoara, Teacher Training Dept, Timisoara, Romania

[2] West Univ Timisoara, Dept Biol & Chem, Timisoara, Romania

[3] Lab Adv Res Environm Protect, Timisoara, Romania

来源：

ACTA BIOCHIMICA POLONICA | 2013年 / 60卷 / 04期

关键词：

glycosidases; structural properties; specific interactions; ALPHA-GLUCOSIDASE; HYDROLYSIS; MECHANISM; SURFACES; SYSTEM;

D O I：

暂无

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：553 / 564

页数：12

共 33 条

[1] The Protein Data Bank [J].