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'''CRYSTAL STRUCTURE OF BOVINE BILE-SALT ACTIVATED LIPASE COMPLEXED WITH TAUROCHOLATE''' | '''CRYSTAL STRUCTURE OF BOVINE BILE-SALT ACTIVATED LIPASE COMPLEXED WITH TAUROCHOLATE''' | ||
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[[Category: Wang, X.]] | [[Category: Wang, X.]] | ||
[[Category: Zhang, X.]] | [[Category: Zhang, X.]] | ||
[[Category: | [[Category: Glycoprotein]] | ||
[[Category: | [[Category: Hydrolase]] | ||
[[Category: | [[Category: Lipid degradation]] | ||
[[Category: | [[Category: Serine esterase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:35:26 2008'' | |||
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Revision as of 07:35, 2 May 2008
CRYSTAL STRUCTURE OF BOVINE BILE-SALT ACTIVATED LIPASE COMPLEXED WITH TAUROCHOLATE
Overview
BACKGROUND: The intestinally located pancreatic enzyme, bile salt activated lipase (BAL), possesses unique activities for digesting different kinds of lipids. It also differs from other lipases in a requirement of bile salts for activity. A structure-based explanation for these unique properties has not been reached so far due to the absence of a three-dimensional structure. RESULTS: The crystal structures of bovine BAL and its complex with taurocholate have been determined at 2.8 A resolution. The overall structure of BAL belongs to the alpha/beta hydrolase fold family. Two bile salt binding sites were found in each BAL molecule within the BAL-taurocholate complex structure. One of these sites is located close to a hairpin loop near the active site. Upon the binding of taurocholate, this loop becomes less mobile and assumes a different conformation. The other bile salt binding site is located remote from the active site. In both structures, BAL forms similar dimers with the active sites facing each other. CONCLUSIONS: Bile salts activate BAL by binding to a relatively short ten-residue loop near the active site, and stabilize the loop in an open conformation. Presumably, this conformational change leads to the formation of the substrate-binding site, as suggested from kinetic data. The BAL dimer observed in the crystal structure may also play a functional role under physiological conditions.
About this Structure
1AQL is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
The crystal structure of bovine bile salt activated lipase: insights into the bile salt activation mechanism., Wang X, Wang CS, Tang J, Dyda F, Zhang XC, Structure. 1997 Sep 15;5(9):1209-18. PMID:9331420 Page seeded by OCA on Fri May 2 10:35:26 2008
