1lpa
From Proteopedia
(New page: 200px<br /> <applet load="1lpa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lpa, resolution 3.04Å" /> '''INTERFACIAL ACTIVAT...) |
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| - | [[Image:1lpa.gif|left|200px]]<br /> | + | [[Image:1lpa.gif|left|200px]]<br /><applet load="1lpa" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1lpa" size=" | + | |
caption="1lpa, resolution 3.04Å" /> | caption="1lpa, resolution 3.04Å" /> | ||
'''INTERFACIAL ACTIVATION OF THE LIPASE-PROCOLIPASE COMPLEX BY MIXED MICELLES REVEALED BY X-RAY CRYSTALLOGRAPHY'''<br /> | '''INTERFACIAL ACTIVATION OF THE LIPASE-PROCOLIPASE COMPLEX BY MIXED MICELLES REVEALED BY X-RAY CRYSTALLOGRAPHY'''<br /> | ||
==Overview== | ==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 | + | 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== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1LPA is a [http://en.wikipedia.org/wiki/Protein_complex 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] with BNG, CA and PLC as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 1LPA is a [http://en.wikipedia.org/wiki/Protein_complex 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] with <scene name='pdbligand=BNG:'>BNG</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=PLC:'>PLC</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LPA OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Triacylglycerol lipase]] | [[Category: Triacylglycerol lipase]] | ||
[[Category: Cambillau, C.]] | [[Category: Cambillau, C.]] | ||
| - | [[Category: Egloff, M | + | [[Category: Egloff, M P.]] |
| - | [[Category: Tilbeurgh, H | + | [[Category: Tilbeurgh, H Van.]] |
[[Category: BNG]] | [[Category: BNG]] | ||
[[Category: CA]] | [[Category: CA]] | ||
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[[Category: hydrolase(carboxylic esterase)]] | [[Category: hydrolase(carboxylic esterase)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:47:10 2008'' |
Revision as of 11:47, 21 February 2008
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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 with , and as ligands. Active as Triacylglycerol lipase, with EC number 3.1.1.3 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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