1lpa
From Proteopedia
(Difference between revisions)
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- | + | ==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]] 3.04Å' scene=''> | |
- | + | == Structural highlights == | |
+ | <table><tr><td colspan='2'>[[1lpa]] is a 2 chain structure with sequence 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LPA FirstGlance]. <br> | ||
+ | </td></tr><tr><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><br> | ||
+ | <tr><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><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://www.rcsb.org/pdb/explore.do?structureId=1lpa RCSB], [http://www.ebi.ac.uk/pdbsum/1lpa PDBsum]</span></td></tr> | ||
+ | <table> | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lp/1lpa_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == 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<ref>PMID:8479519</ref> | |
- | + | ||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
==See Also== | ==See Also== | ||
*[[Lipase|Lipase]] | *[[Lipase|Lipase]] | ||
*[[Molecular Playground/Pancreatic Lipase|Molecular Playground/Pancreatic Lipase]] | *[[Molecular Playground/Pancreatic Lipase|Molecular Playground/Pancreatic Lipase]] | ||
- | + | == References == | |
- | == | + | <references/> |
- | < | + | __TOC__ |
+ | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] |
Revision as of 16:21, 29 September 2014
INTERFACIAL ACTIVATION OF THE LIPASE-PROCOLIPASE COMPLEX BY MIXED MICELLES REVEALED BY X-RAY CRYSTALLOGRAPHY
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