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4x93

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Revision as of 21:18, 12 April 2023

Crystal structure of Lysosomal Phospholipase A2 crystallized in the presence of methyl arachidonyl fluorophosphonate (tetragonal form)

Structural highlights

4x93 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PAG15_HUMAN Has transacylase and calcium-independent phospholipase A2 activity. Catalyzes the formation of 1-O-acyl-N-acetylsphingosine and the concomitant release of a lyso-phospholipid (By similarity). May have weak lysophospholipase activity.

Publication Abstract from PubMed

Lysosomal phospholipase A2 (LPLA2) and lecithin:cholesterol acyltransferase (LCAT) belong to a structurally uncharacterized family of key lipid-metabolizing enzymes responsible for lung surfactant catabolism and for reverse cholesterol transport, respectively. Whereas LPLA2 is predicted to underlie the development of drug-induced phospholipidosis, somatic mutations in LCAT cause fish eye disease and familial LCAT deficiency. Here we describe several high-resolution crystal structures of human LPLA2 and a low-resolution structure of LCAT that confirms its close structural relationship to LPLA2. Insertions in the alpha/beta hydrolase core of LPLA2 form domains that are responsible for membrane interaction and binding the acyl chains and head groups of phospholipid substrates. The LCAT structure suggests the molecular basis underlying human disease for most of the known LCAT missense mutations, and paves the way for rational development of new therapeutics to treat LCAT deficiency, atherosclerosis and acute coronary syndrome.

Structure and function of lysosomal phospholipase A2 and lecithin:cholesterol acyltransferase.,Glukhova A, Hinkovska-Galcheva V, Kelly R, Abe A, Shayman JA, Tesmer JJ Nat Commun. 2015 Mar 2;6:6250. doi: 10.1038/ncomms7250. PMID:25727495^[1]

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

References

↑ Glukhova A, Hinkovska-Galcheva V, Kelly R, Abe A, Shayman JA, Tesmer JJ. Structure and function of lysosomal phospholipase A2 and lecithin:cholesterol acyltransferase. Nat Commun. 2015 Mar 2;6:6250. doi: 10.1038/ncomms7250. PMID:25727495 doi:http://dx.doi.org/10.1038/ncomms7250

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4x93"

Categories: Homo sapiens | Large Structures | Glukhova A | Tesmer JJG

@@ Line 3: / Line 3: @@
 <StructureSection load='4x93' size='340' side='right'caption='[[4x93]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4x93]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X93 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X93 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4x93]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X93 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X93 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PE8:3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL'>PE8</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PE8:3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL'>PE8</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4x90|4x90]], [[4x91|4x91]], [[4x92|4x92]], [[4x94|4x94]], [[4x95|4x95]], [[4x96|4x96]], [[4x97|4x97]]</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=4x93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x93 OCA], [https://pdbe.org/4x93 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x93 RCSB], [https://www.ebi.ac.uk/pdbsum/4x93 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x93 ProSAT]</span></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PLA2G15, LYPLA3, UNQ341/PRO540 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4x93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x93 OCA], [http://pdbe.org/4x93 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4x93 RCSB], [http://www.ebi.ac.uk/pdbsum/4x93 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4x93 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PAG15_HUMAN PAG15_HUMAN]] Has transacylase and calcium-independent phospholipase A2 activity. Catalyzes the formation of 1-O-acyl-N-acetylsphingosine and the concomitant release of a lyso-phospholipid (By similarity). May have weak lysophospholipase activity.
+[https://www.uniprot.org/uniprot/PAG15_HUMAN PAG15_HUMAN] Has transacylase and calcium-independent phospholipase A2 activity. Catalyzes the formation of 1-O-acyl-N-acetylsphingosine and the concomitant release of a lyso-phospholipid (By similarity). May have weak lysophospholipase activity.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 27: / Line 25: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Glukhova, A]]
+[[Category: Glukhova A]]
-[[Category: Tesmer, J J.G]]
+[[Category: Tesmer JJG]]
-[[Category: Acyltransferase]]
-[[Category: Esterase]]
-[[Category: Hydrolase]]
-[[Category: Phospholipase]]
-[[Category: Transferase]]

4x93

From Proteopedia

Revision as of 21:18, 12 April 2023

Crystal structure of Lysosomal Phospholipase A2 crystallized in the presence of methyl arachidonyl fluorophosphonate (tetragonal form)

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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