Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1CBG

THE CRYSTAL STRUCTURE OF A CYANOGENIC BETA-GLUCOSIDASE FROM WHITE CLOVER (TRIFOLIUM REPENS L.), A FAMILY 1 GLYCOSYL-HYDROLASE

Summary for 1CBG
Entry DOI10.2210/pdb1cbg/pdb
DescriptorCYANOGENIC BETA-GLUCOSIDASE (2 entities in total)
Functional Keywordscyanogenic beta-glucosidase, hydrolase (o-glycosyl)
Biological sourceTrifolium repens (white clover)
Total number of polymer chains1
Total formula weight56419.66
Authors
Barrett, T.E.,Suresh, C.G.,Tolley, S.P.,Hughes, M.A. (deposition date: 1995-07-31, release date: 1995-10-15, Last modification date: 2024-10-23)
Primary citationBarrett, T.,Suresh, C.G.,Tolley, S.P.,Dodson, E.J.,Hughes, M.A.
The crystal structure of a cyanogenic beta-glucosidase from white clover, a family 1 glycosyl hydrolase.
Structure, 3:951-960, 1995
Cited by
PubMed Abstract: beta-glucosidases occur in a variety of organisms and catalyze the hydrolysis of aryl and alkyl-beta-D-glucosides as well as glucosides with only a carbohydrate moiety (such as cellobiose). The cyanogenic beta-glucosidase from white clover (subsequently referred to as CBG) is responsible for the cleavage of cyanoglucosides. Both CBG and the cyanoglucosides occur within the plant cell wall where they are found in separate compartments and only come into contact when the leaf tissue experiences mechanical damage. This results in the eventual production of hydrogen cyanide which acts as a deterrent to grazing animals. beta-glucosidases have been assigned to particular glycosyl hydrolase families on the basis of sequence similarity; this classification has placed CBG in family 1 (there are a total of over 40 families) for which a three-dimensional structure has so far not been determined. This is the first report of the three-dimensional structure of a glycosyl hydrolase from family 1.
PubMed: 8535788
DOI: 10.1016/S0969-2126(01)00229-5
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.15 Å)
Structure validation

236371

PDB entries from 2025-05-21

PDB statisticsPDBj update infoContact PDBjnumon