Progress in predicting protein function from structure: unique features of O-glycosidases.
The Structural Genomics Initiative promises to deliver between 10,000 and 20,000 new protein structures within the next ten years. One challenge will be to predict the functions of these proteins from their structures. Since the newly solved structures will be enriched in proteins with little sequence identity to those whose structures are known, new methods for predicting function will be required. Here we describe the unique structural characteristics of O-glycosidases, enzymes that hydrolyze O-glycosidic bonds between carbohydrates. O-glycosidase function has evolved independently many times and enzymes that carry out this function are represented by a large number of different folds. We show that O-glycosidases none-the-less have characteristic structural features that cross sequence and fold families. The electrostatic surfaces of this class of enzymes are particularly distinctive. We also demonstrate that accurate prediction of O-glycosidase function from structure is possible.
Stawiski
E W
EW
Departments of Chemistry and Biochemistry and Molecular, Cell and Developmental Biology, University of California, Santa Cruz, CA 95060, USA.
Mandel-Gutfreund
Y
Y
Lowenthal
A C
AC
Gregoret
L M
LM
D005796:Genes; D023281:Genomics; D006026:Glycoside Hydrolases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D006027:Glycosides / Q000378:metabolism; D006801:Humans; D006868:Hydrolysis; D007700:Kinetics; D016571:Neural Networks, Computer; D017384:Sequence Deletion; D012984:Software; D055672:Static Electricity; D013329:Structure-Activity Relationship
D006027:Glycosides; D006026:Glycoside Hydrolases