1lpa
From Proteopedia
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| - | [[Image:1lpa.gif|left|200px]] | + | [[Image:1lpa.gif|left|200px]] |
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| - | '''INTERFACIAL ACTIVATION OF THE LIPASE-PROCOLIPASE COMPLEX BY MIXED MICELLES REVEALED BY X-RAY CRYSTALLOGRAPHY''' | + | {{Structure |
| + | |PDB= 1lpa |SIZE=350|CAPTION= <scene name='initialview01'>1lpa</scene>, resolution 3.04Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=BNG:B-NONYLGLUCOSIDE'>BNG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=PLC:DIUNDECYL PHOSPHATIDYL CHOLINE'>PLC</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= | ||
| + | }} | ||
| + | |||
| + | '''INTERFACIAL ACTIVATION OF THE LIPASE-PROCOLIPASE COMPLEX BY MIXED MICELLES REVEALED BY X-RAY CRYSTALLOGRAPHY''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1LPA is a [ | + | 1LPA is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LPA OCA]. |
==Reference== | ==Reference== | ||
| - | Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography., van Tilbeurgh H, Egloff MP, Martinez C, Rugani N, Verger R, Cambillau C, Nature. 1993 Apr 29;362(6423):814-20. PMID:[http:// | + | Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography., van Tilbeurgh H, Egloff MP, Martinez C, Rugani N, Verger R, Cambillau C, Nature. 1993 Apr 29;362(6423):814-20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8479519 8479519] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: hydrolase(carboxylic esterase)]] | [[Category: hydrolase(carboxylic 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 12:33:31 2008'' |
Revision as of 10:33, 20 March 2008
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| , resolution 3.04Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| Activity: | Triacylglycerol lipase, with EC number 3.1.1.3 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
INTERFACIAL ACTIVATION OF THE LIPASE-PROCOLIPASE COMPLEX BY MIXED MICELLES REVEALED BY X-RAY CRYSTALLOGRAPHY
Contents |
Overview
The three-dimensional structure of the lipase-procolipase complex, co-crystallized with mixed micelles of phosphatidylcholine and bile salt, has been determined at 3 A resolution by X-ray crystallography. The lid, a surface helix covering the catalytic triad of lipase, adopts a totally different conformation which allows phospholipid to bind to the enzyme's active site. The open lid is an essential component of the active site and interacts with procolipase. Together they form the lipid-water interface binding site. This reorganization of the lid structure provokes a second drastic conformational change in an active site loop, which in its turn creates the oxyanion hole (induced fit).
Disease
Known disease associated with this structure: Pancreatic lipase deficiency OMIM:[246600]
About this Structure
1LPA is a Protein complex structure of sequences from Homo sapiens and Sus scrofa. Full crystallographic information is available from OCA.
Reference
Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography., van Tilbeurgh H, Egloff MP, Martinez C, Rugani N, Verger R, Cambillau C, Nature. 1993 Apr 29;362(6423):814-20. PMID:8479519
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