Crystal structure of the catalytic domain of human bile salt activated lipase.
Article Details
- CitationCopy to clipboard
Terzyan S, Wang CS, Downs D, Hunter B, Zhang XC
Crystal structure of the catalytic domain of human bile salt activated lipase.
Protein Sci. 2000 Sep;9(9):1783-90.
- PubMed ID
- 11045623 [ View in PubMed]
- 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).