Terzyan_2000_Protein.Sci_9_1783

Reference

Title : Crystal structure of the catalytic domain of human bile salt activated lipase - Terzyan_2000_Protein.Sci_9_1783
Author(s) : Terzyan S , Wang CS , Downs D , Hunter B , Zhang XC
Ref : Protein Science , 9 :1783 , 2000
Abstract :

Bile-salt activated lipase (BAL) is a pancreatic enzyme that digests a variety of lipids in the small intestine. A distinct property of BAL is its dependency on bile salts in hydrolyzing substrates of long acyl chains or bulky alcoholic motifs. A crystal structure of the catalytic domain of human BAL (residues 1-538) with two surface mutations (N186D and A298D), which were introduced in attempting to facilitate crystallization, has been determined at 2.3 A resolution. The crystal form belongs to space group P2(1)2(1)2(1) with one monomer per asymmetric unit, and the protein shows an alpha/beta hydrolase fold. In the absence of bound bile salt molecules, the protein possesses a preformed catalytic triad and a functional oxyanion hole. Several surface loops around the active site are mobile, including two loops potentially involved in substrate binding (residues 115-125 and 270-285).

PubMedSearch : Terzyan_2000_Protein.Sci_9_1783
PubMedID: 11045623
Gene_locus related to this paper: human-CEL

Related information

Gene_locus human-CEL
Family human-CEL    Cholesterol_esterase
Structure human-CEL    Cholesterol_esterase    1F6W

Citations formats

Terzyan S, Wang CS, Downs D, Hunter B, Zhang XC (2000)
Crystal structure of the catalytic domain of human bile salt activated lipase
Protein Science 9 :1783

Terzyan S, Wang CS, Downs D, Hunter B, Zhang XC (2000)
Protein Science 9 :1783