1f6w
From Proteopedia
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'''STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN BILE SALT ACTIVATED LIPASE''' | '''STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN BILE SALT ACTIVATED LIPASE''' | ||
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[[Category: Terzyan, S.]] | [[Category: Terzyan, S.]] | ||
[[Category: Zhang, X.]] | [[Category: Zhang, X.]] | ||
| - | [[Category: | + | [[Category: Bile salt activated lipase]] |
| - | [[Category: | + | [[Category: Catalytic domain]] |
| - | [[Category: | + | [[Category: Esterase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:58:30 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 12:58, 2 May 2008
STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN BILE SALT ACTIVATED LIPASE
Overview
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).
About this Structure
1F6W is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the catalytic domain of human bile salt activated lipase., Terzyan S, Wang CS, Downs D, Hunter B, Zhang XC, Protein Sci. 2000 Sep;9(9):1783-90. PMID:11045623 Page seeded by OCA on Fri May 2 15:58:30 2008
