1F6W

STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN BILE SALT ACTIVATED LIPASE

Summary for 1F6W

• Entry DOI: 10.2210/pdb1f6w/pdb
• Related: 1AKN
• Descriptor: BILE SALT ACTIVATED LIPASE (2 entities in total)
• Functional Keywords: bile salt activated lipase, esterase, catalytic domain, hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P19835
• Total number of polymer chains: 1
• Total formula weight: 58826.69

Authors

Terzyan, S.,Zhang, X. (deposition date: 2000-06-23, release date: 2000-10-18, Last modification date: 2024-10-30)

Primary citation

Terzyan, S.,Wang, C.S.,Downs, D.,Hunter, B.,Zhang, X.C.
Crystal structure of the catalytic domain of human bile salt activated lipase.
Protein Sci., 9:1783-1790, 2000

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).

PubMed: 11045623

Experimental method

X-RAY DIFFRACTION (2.3 Å)