1aql: Difference between revisions
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[[Image:1aql.gif|left|200px]] | [[Image:1aql.gif|left|200px]] | ||
'''CRYSTAL STRUCTURE OF BOVINE BILE-SALT ACTIVATED LIPASE COMPLEXED WITH TAUROCHOLATE''' | {{Structure | ||
|PDB= 1aql |SIZE=350|CAPTION= <scene name='initialview01'>1aql</scene>, resolution 2.8Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> and <scene name='pdbligand=TCH:TAUROCHOLIC ACID'>TCH</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Sterol_esterase Sterol esterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.13 3.1.1.13] | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF BOVINE BILE-SALT ACTIVATED LIPASE COMPLEXED WITH TAUROCHOLATE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1AQL is a [ | 1AQL 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=1AQL 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: serine esterase]] | [[Category: serine esterase]] | ||
''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 10:01:02 2008'' | ||
Revision as of 08:01, 20 March 2008
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| 1aql, resolution 2.8Å | |||||||||||||
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| Ligands: | NAG and TCH | ||||||||||||
| Activity: | Sterol esterase, with EC number 3.1.1.13 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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
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