1lpa

From Proteopedia

(Difference between revisions)

Revision as of 06:45, 29 November 2017

INTERFACIAL ACTIVATION OF THE LIPASE-PROCOLIPASE COMPLEX BY MIXED MICELLES REVEALED BY X-RAY CRYSTALLOGRAPHY

Structural highlights

1lpa is a 2 chain structure with sequence from Human and Pig. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Activity:	Triacylglycerol lipase, with EC number 3.1.1.3
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[COL_PIG] Colipase is a cofactor of pancreatic lipase. It allows the lipase to anchor itself to the lipid-water interface. Without colipase the enzyme is washed off by bile salts, which have an inhibitory effect on the lipase. Enterostatin has a biological activity as a satiety signal.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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).

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ van Tilbeurgh H, Egloff MP, Martinez C, Rugani N, Verger R, Cambillau C. Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography. Nature. 1993 Apr 29;362(6423):814-20. PMID:8479519 doi:http://dx.doi.org/10.1038/362814a0

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1lpa"

@@ Line 1: / Line 1: @@
 ==INTERFACIAL ACTIVATION OF THE LIPASE-PROCOLIPASE COMPLEX BY MIXED MICELLES REVEALED BY X-RAY CRYSTALLOGRAPHY==
 <StructureSection load='1lpa' size='340' side='right' caption='[[1lpa]], [[Resolution|resolution]] 3.04&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BNG:B-NONYLGLUCOSIDE'>BNG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PLC:DIUNDECYL+PHOSPHATIDYL+CHOLINE'>PLC</scene></td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lpa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lpa OCA], [http://pdbe.org/1lpa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lpa RCSB], [http://www.ebi.ac.uk/pdbsum/1lpa PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lpa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lpa OCA], [http://pdbe.org/1lpa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lpa RCSB], [http://www.ebi.ac.uk/pdbsum/1lpa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1lpa ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 30: / Line 31: @@
 ==See Also==
-*[[Lipase|Lipase]]
 *[[Molecular Playground/Pancreatic Lipase|Molecular Playground/Pancreatic Lipase]]
 == References ==

1lpa

From Proteopedia

Revision as of 06:45, 29 November 2017

INTERFACIAL ACTIVATION OF THE LIPASE-PROCOLIPASE COMPLEX BY MIXED MICELLES REVEALED BY X-RAY CRYSTALLOGRAPHY

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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