1gpl

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (11:23, 27 March 2024) (edit) (undo)
 
(14 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1gpl.gif|left|200px]]
 
-
{{Structure
+
==RP2 LIPASE==
-
|PDB= 1gpl |SIZE=350|CAPTION= <scene name='initialview01'>1gpl</scene>, resolution 2.01&Aring;
+
<StructureSection load='1gpl' size='340' side='right'caption='[[1gpl]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
-
|SITE= <scene name='pdbsite=CAT:Catalytic+Triad.+The+Nucleophile+SER+152+Is+Located+In+A+...'>CAT</scene>
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>
+
<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>
-
|ACTIVITY= <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='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>
-
|GENE=
+
<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>
-
|DOMAIN=
+
<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>
-
|RELATEDENTRY=
+
</table>
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gpl OCA], [http://www.ebi.ac.uk/pdbsum/1gpl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gpl RCSB]</span>
+
== 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>
-
'''RP2 LIPASE'''
+
==See Also==
-
 
+
*[[Lipase 3D Structures|Lipase 3D Structures]]
-
 
+
== References ==
-
==Overview==
+
<references/>
-
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 probably exists under a permanent open conformation. Therefore, the phenomenon of interfacial activation in HPL is not only due to the presence of a full-length lid domain but also to other structural elements which probably allow the existence of stabilized closed and open conformations of the lid. GPLRP2(+lid) phospholipase activity is significantly reduced as compared to GPLRP2, whereas its lipase activity remains at the same level. Therefore, the lid domain plays a major role in substrate selectivity and can be considered as part of the active site. However, the presence of a full-length lid domain is not sufficient to explain the absence of phospholipase activity in HPL since HPL(-lid) does not display any phospholipase activity. We also produced a chimeric GPLRP2 mutant in which the C-terminal domain was substituted by the HPL C-terminal domain. The colipase effects, i.e., anchoring and stabilization of the lipase at the interface, are clearly observed with the chimera, whereas GPLRP2 is insensitive to colipase. The kinetic characterization of this chimera reveals for the first time that the interfacial stability of pancreatic lipases depends on the structure of the C-terminal domain.
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
-
1GPL is a [[Single protein]] structure of sequence from [http://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].
+
-
 
+
-
==Reference==
+
-
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://www.ncbi.nlm.nih.gov/pubmed/8993339 8993339]
+
[[Category: Cavia porcellus]]
[[Category: Cavia porcellus]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Triacylglycerol lipase]]
+
[[Category: Cambillau C]]
-
[[Category: Cambillau, C.]]
+
[[Category: Withers-Martinez C]]
-
[[Category: Withers-Martinez, C.]]
+
-
[[Category: chimeric]]
+
-
[[Category: glycoprotein]]
+
-
[[Category: hydrolase]]
+
-
[[Category: lipid degradation]]
+
-
[[Category: pancrea]]
+
-
[[Category: serine esterase]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:48:52 2008''
+

Current revision

RP2 LIPASE

PDB ID 1gpl

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1gpl"
Personal tools