1gpl: Difference between revisions

Latest revision as of 11:23, 27 March 2024

RP2 LIPASE

Structural highlights

1gpl is a 1 chain structure with sequence from Cavia porcellus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.01Å
Ligands:	CA
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LIPP_HUMAN LIPR2_CAVPO Lipase that primarily hydrolyzes triglycerides and galactosylglycerides (PubMed:8490016, PubMed:17401110, PubMed:20083229, PubMed:8939760). In neonates, may play a major role in pancreatic digestion of dietary fats such as milk fat globules enriched in long-chain triglycerides (By similarity). Hydrolyzes short-, medium- and long-chain fatty acyls in triglycerides without apparent positional specificity (PubMed:8490016, PubMed:8939760). Can completely deacylate triacylglycerols (By similarity). When the liver matures and bile salt synthesis increases, likely functions mainly as a galactolipase and monoacylglycerol lipase. Hydrolyzes monogalactosyldiglycerols (MGDG) and digalactosyldiacylglycerols (DGDG) present in a plant-based diet, releasing long-chain polyunsaturated fatty acids (PubMed:20083229, PubMed:8939760). Hydrolyzes medium- and long-chain fatty acyls in galactolipids. May act together with LIPF to hydrolyze partially digested triglycerides (By similarity). Hydrolyzes long-chain monoglycerides with high efficiency. In cytotoxic T cells, contributes to perforin-dependent cell lysis, but is unlikely to mediate direct cytotoxicity (By similarity). Also has low phospholipase activity (By similarity). In neurons, required for the localization of the phospholipid 1-oleoyl-2-palmitoyl-PC (OPPC) to neurite tips through acyl chain remodeling of membrane phospholipids (By similarity). The resulting OPPC-rich lipid membrane domain recruits the t-SNARE protein STX4 by selectively interacting with the STX4 transmembrane domain and this promotes surface expression of the dopamine transporter SLC6A3/DAT at neurite tips by facilitating fusion of SLC6A3-containing transport vesicles with the plasma membrane (By similarity).[UniProtKB:P17892][UniProtKB:P54317][UniProtKB:P54318]^[1] ^[2] ^[3] ^[4]

Evolutionary Conservation

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

References

↑ Eydoux C, De Caro J, Ferrato F, Boullanger P, Lafont D, Laugier R, Carrière F, De Caro A. Further biochemical characterization of human pancreatic lipase-related protein 2 expressed in yeast cells. J Lipid Res. 2007 Jul;48(7):1539-49. PMID:17401110 doi:10.1194/jlr.M600486-JLR200
↑ Amara S, Barouh N, Lecomte J, Lafont D, Robert S, Villeneuve P, De Caro A, Carriere F. Lipolysis of natural long chain and synthetic medium chain galactolipids by pancreatic lipase-related protein 2. Biochim Biophys Acta. 2010 Apr;1801(4):508-16. doi: 10.1016/j.bbalip.2010.01.003., Epub 2010 Jan 18. PMID:20083229 doi:https://dx.doi.org/10.1016/j.bbalip.2010.01.003
↑ Hjorth A, Carrière F, Cudrey C, Wöldike H, Boel E, Lawson DM, Ferrato F, Cambillau C, Dodson GG, Thim L, et al.. A structural domain (the lid) found in pancreatic lipases is absent in the guinea pig (phospho)lipase. Biochemistry. 1993 May 11;32(18):4702-7. PMID:8490016 doi:10.1021/bi00069a003
↑ Withers-Martinez C, Carriere F, Verger R, Bourgeois D, Cambillau C. A pancreatic lipase with a phospholipase A1 activity: crystal structure of a chimeric pancreatic lipase-related protein 2 from guinea pig. Structure. 1996 Nov 15;4(11):1363-74. PMID:8939760

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Eydoux C, De Caro J, Ferrato F, Boullanger P, Lafont D, Laugier R, Carrière F, De Caro A. Further biochemical characterization of human pancreatic lipase-related protein 2 expressed in yeast cells. J Lipid Res. 2007 Jul;48(7):1539-49. PMID:17401110 doi:10.1194/jlr.M600486-JLR200

[2] Amara S, Barouh N, Lecomte J, Lafont D, Robert S, Villeneuve P, De Caro A, Carriere F. Lipolysis of natural long chain and synthetic medium chain galactolipids by pancreatic lipase-related protein 2. Biochim Biophys Acta. 2010 Apr;1801(4):508-16. doi: 10.1016/j.bbalip.2010.01.003., Epub 2010 Jan 18. PMID:20083229 doi:https://dx.doi.org/10.1016/j.bbalip.2010.01.003

[3] Hjorth A, Carrière F, Cudrey C, Wöldike H, Boel E, Lawson DM, Ferrato F, Cambillau C, Dodson GG, Thim L, et al.. A structural domain (the lid) found in pancreatic lipases is absent in the guinea pig (phospho)lipase. Biochemistry. 1993 May 11;32(18):4702-7. PMID:8490016 doi:10.1021/bi00069a003

[4] Withers-Martinez C, Carriere F, Verger R, Bourgeois D, Cambillau C. A pancreatic lipase with a phospholipase A1 activity: crystal structure of a chimeric pancreatic lipase-related protein 2 from guinea pig. Structure. 1996 Nov 15;4(11):1363-74. PMID:8939760

[1]

[2]

[3]

[4]

@@ Line 1: / Line 1: @@
-[[Image:1gpl.gif|left|200px]]<br />
-<applet load="1gpl" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1gpl, resolution 2.01&Aring;" />
-'''RP2 LIPASE'''<br />
-==Overview==
+==RP2 LIPASE==
-We designed chimeric mutants by exchanging the lid domains of the, classical human pancreatic lipase (HPL) and the guinea pig pancreatic, lipase related protein 2 (GPLRP2). This latter enzyme possesses naturally, a large deletion within the lid domain and is not activated by lipid/water, interfaces. Furthermore, GPLRP2 exhibits phospholipase A1 and lipase, activities in the same order of magnitude, whereas HPL has no significant, phospholipase activity and displays a clear interfacial activation. An HPL, mutant [HPL(-lid)] with GPLRP2 mini-lid domain does not display, interfacial activation. Its specific activity toward triglycerides is, however, dramatically reduced. A GPLRP2 mutant [GPLRP2(+lid)] with HPL, full-length lid domain is not interfacially activated, and its lid domain, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?8993339 (full description)]]
+<StructureSection load='1gpl' size='340' side='right'caption='[[1gpl]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1gpl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cavia_porcellus Cavia porcellus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GPL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GPL FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.01&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gpl OCA], [https://pdbe.org/1gpl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gpl RCSB], [https://www.ebi.ac.uk/pdbsum/1gpl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gpl ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/LIPP_HUMAN LIPP_HUMAN] [https://www.uniprot.org/uniprot/LIPR2_CAVPO LIPR2_CAVPO] Lipase that primarily hydrolyzes triglycerides and galactosylglycerides (PubMed:8490016, PubMed:17401110, PubMed:20083229, PubMed:8939760). In neonates, may play a major role in pancreatic digestion of dietary fats such as milk fat globules enriched in long-chain triglycerides (By similarity). Hydrolyzes short-, medium- and long-chain fatty acyls in triglycerides without apparent positional specificity (PubMed:8490016, PubMed:8939760). Can completely deacylate triacylglycerols (By similarity). When the liver matures and bile salt synthesis increases, likely functions mainly as a galactolipase and monoacylglycerol lipase. Hydrolyzes monogalactosyldiglycerols (MGDG) and digalactosyldiacylglycerols (DGDG) present in a plant-based diet, releasing long-chain polyunsaturated fatty acids (PubMed:20083229, PubMed:8939760). Hydrolyzes medium- and long-chain fatty acyls in galactolipids. May act together with LIPF to hydrolyze partially digested triglycerides (By similarity). Hydrolyzes long-chain monoglycerides with high efficiency. In cytotoxic T cells, contributes to perforin-dependent cell lysis, but is unlikely to mediate direct cytotoxicity (By similarity). Also has low phospholipase activity (By similarity). In neurons, required for the localization of the phospholipid 1-oleoyl-2-palmitoyl-PC (OPPC) to neurite tips through acyl chain remodeling of membrane phospholipids (By similarity). The resulting OPPC-rich lipid membrane domain recruits the t-SNARE protein STX4 by selectively interacting with the STX4 transmembrane domain and this promotes surface expression of the dopamine transporter SLC6A3/DAT at neurite tips by facilitating fusion of SLC6A3-containing transport vesicles with the plasma membrane (By similarity).[UniProtKB:P17892][UniProtKB:P54317][UniProtKB:P54318]<ref>PMID:17401110</ref> <ref>PMID:20083229</ref> <ref>PMID:8490016</ref> <ref>PMID:8939760</ref>
+== 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/gp/1gpl_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/main_output.php?pdb_ID=1gpl ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-GPL is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Cavia_porcellus Cavia porcellus]] with CA as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GPL OCA]].
+*[[Lipase 3D Structures|Lipase 3D Structures]]
+== References ==
-==Reference==
+<references/>
-Pancreatic lipase structure-function relationships by domain exchange., Carriere F, Thirstrup K, Hjorth S, Ferrato F, Nielsen PF, Withers-Martinez C, Cambillau C, Boel E, Thim L, Verger R, Biochemistry. 1997 Jan 7;36(1):239-48. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8993339 8993339]
+__TOC__
+</StructureSection>
 [[Category: Cavia porcellus]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Cambillau, C.]]
+[[Category: Cambillau C]]
-[[Category: Withers-Martinez, C.]]
+[[Category: Withers-Martinez C]]
-[[Category: CA]]
-[[Category: chimeric]]
-[[Category: glycoprotein]]
-[[Category: hydrolase]]
-[[Category: lipid degradation]]
-[[Category: pancreas]]
-[[Category: serine esterase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 19:44:32 2007''

1gpl: Difference between revisions

Latest revision as of 11:23, 27 March 2024

RP2 LIPASE

Structural highlights

Function

Evolutionary Conservation

See Also

References

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