β‐Helical catalytic domains in glycoside hydrolase families 49, 55 and 87: domain architecture, modelling and assignment of catalytic residues

FEBS Letters

Franco, Octávio L¹  Rigden, Daniel J¹ 

[1] Embrapa Genetic Resources and Biotechnology, Cenargen/Embrapa, S.A.I.N. Parque Rural, Final W5, Asa Norte, 70770-900 Brası́lia DF, Brazil

关键词: Glycosidase;    Iterative database search;    Fold recognition;    Evolutionary relationship;   

DOI  :  10.1016/S0014-5793(02)03490-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

X-ray crystallography and bioinformatics studies reveal a tendency for the right-handed β-helix domain architecture to be associated with carbohydrate binding proteins. Here we demonstrate the presence of catalytic β-helix domains in glycoside hydrolase (GH) families 49, 55 and 87 and provide evidence for their sharing a common evolutionary ancestor with two structurally characterized GH families, numbers 28 and 82. This domain assignment helps assign catalytic residues to each family. Further analysis of domain architecture reveals the association of carbohydrate binding modules with catalytic GH β-helices, as well as an unexpected pair of β-helix domains in GH family 55.

【 授权许可】

Unknown