Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The three-dimensional structure of a catalytically competent glycosyl-enzyme intermediate of a retaining beta-1,4-glycanase has been determined at a resolution of 1.8 A by X-ray diffraction. A fluorinated slow substrate forms an alpha-D-glycopyranosyl linkage to one of the two invariant carboxylates, Glu 233, as supported in solution by 19F-NMR studies. The resulting ester linkage is coplanar with the cyclic oxygen of the proximal saccharide and is inferred to form a strong hydrogen bond with the 2-hydroxyl of that saccharide unit in natural substrates. The active-site architecture of this covalent intermediate gives insights into both the classical double-displacement catalytic mechanism and the basis for the enzyme's specificity.
Crystallographic observation of a covalent catalytic intermediate in a beta-glycosidase.,White A, Tull D, Johns K, Withers SG, Rose DR Nat Struct Biol. 1996 Feb;3(2):149-54. PMID:8564541[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ White A, Tull D, Johns K, Withers SG, Rose DR. Crystallographic observation of a covalent catalytic intermediate in a beta-glycosidase. Nat Struct Biol. 1996 Feb;3(2):149-54. PMID:8564541
