1akn
From Proteopedia
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| - | [[Image:1akn.gif|left|200px]] | + | [[Image:1akn.gif|left|200px]] |
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| - | '''STRUCTURE OF BILE-SALT ACTIVATED LIPASE''' | + | {{Structure |
| + | |PDB= 1akn |SIZE=350|CAPTION= <scene name='initialview01'>1akn</scene>, resolution 2.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''STRUCTURE OF BILE-SALT ACTIVATED LIPASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1AKN is a [ | + | 1AKN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AKN OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9331420 9331420] |
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: signal]] | [[Category: signal]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:58:52 2008'' |
Revision as of 07:58, 20 March 2008
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| , resolution 2.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Triacylglycerol lipase, with EC number 3.1.1.3 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF BILE-SALT ACTIVATED LIPASE
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
1AKN 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
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