1F6W

STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN BILE SALT ACTIVATED LIPASE

1F6W の概要

• エントリーDOI: 10.2210/pdb1f6w/pdb
• 関連するPDBエントリー: 1AKN
• 分子名称: BILE SALT ACTIVATED LIPASE (2 entities in total)
• 機能のキーワード: bile salt activated lipase, esterase, catalytic domain, hydrolase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted: P19835
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 58826.69

構造登録者

Terzyan, S.,Zhang, X. (登録日: 2000-06-23, 公開日: 2000-10-18, 最終更新日: 2024-10-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.3 Å)