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| | ==Crystal structure of human lysophosphatidic acid phosphatase type 6 complexed with L-(+)-tartrate== | | ==Crystal structure of human lysophosphatidic acid phosphatase type 6 complexed with L-(+)-tartrate== |
| - | <StructureSection load='4job' size='340' side='right' caption='[[4job]], [[Resolution|resolution]] 2.17Å' scene=''> | + | <StructureSection load='4job' size='340' side='right'caption='[[4job]], [[Resolution|resolution]] 2.17Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4job]] is a 1 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=4JOB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JOB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4job]] is a 1 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=4JOB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JOB FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4joc|4joc]], [[4jod|4jod]]</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=4job FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4job OCA], [https://pdbe.org/4job PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4job RCSB], [https://www.ebi.ac.uk/pdbsum/4job PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4job ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACP6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acid_phosphatase Acid phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.2 3.1.3.2] </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=4job FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4job OCA], [http://pdbe.org/4job PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4job RCSB], [http://www.ebi.ac.uk/pdbsum/4job PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4job ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PPA6_HUMAN PPA6_HUMAN]] Hydrolyzes lysophosphatidic acid to monoacylglycerol.<ref>PMID:10506173</ref> | + | [https://www.uniprot.org/uniprot/PPA6_HUMAN PPA6_HUMAN] Hydrolyzes lysophosphatidic acid to monoacylglycerol.<ref>PMID:10506173</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Acid phosphatase|Acid phosphatase]] | + | *[[Acid phosphatase 3D structures|Acid phosphatase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Acid phosphatase]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Human]] | + | [[Category: Large Structures]] |
| - | [[Category: Li, J]] | + | [[Category: Li J]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Mitochondria]]
| + | |
| - | [[Category: Rossmann fold]]
| + | |
| Structural highlights
Function
PPA6_HUMAN Hydrolyzes lysophosphatidic acid to monoacylglycerol.[1]
Publication Abstract from PubMed
Lysophosphatidic acid (LPA) is an important bioactive phospholipid involved in cell signaling through Gprotein-coupled receptors pathways. It is also involved in balancing the lipid composition inside the cell, and modulates the function of lipid rafts as an intermediate in phospholipid metabolism. Because of its involvement in these important processes, LPA degradation needs to be regulated as precisely as its production. Lysophosphatidic acid phosphatase type 6 (ACP6) is an LPA-specific acid phosphatase that hydrolyzes LPA to monoacylglycerol (MAG) and phosphate. Here, we report three crystal structures of human ACP6 in complex with malonate, L-(+)-tartrate and tris, respectively. Our analyses revealed that ACP6 possesses a highly conserved Rossmann-foldlike body domain as well as a less conserved cap domain. The vast hydrophobic substrate-binding pocket, which is located between those two domains, is suitable for accommodating LPA, and its shape is different from that of other histidine acid phosphatases, a fact that is consistent with the observed difference in substrate preferences. Our analysis of the binding of three molecules in the active site reveals the involvement of six conserved and crucial residues in binding of the LPA phosphate group and its catalysis. The structure also indicates a water-supplying channel for substrate hydrolysis. Our structural data are consistent with the fact that the enzyme is active as a monomer. In combination with additional mutagenesis and enzyme activity studies, our structural data provide important insights into substrate recognition and the mechanism for catalytic activity of ACP6.
Crystal structures and biochemical studies of human lysophosphatidic acid phosphatase type 6.,Li J, Dong Y, Lu X, Wang L, Peng W, Zhang XC, Rao Z Protein Cell. 2013 Jun 26. PMID:23807634[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hiroyama M, Takenawa T. Isolation of a cDNA encoding human lysophosphatidic acid phosphatase that is involved in the regulation of mitochondrial lipid biosynthesis. J Biol Chem. 1999 Oct 8;274(41):29172-80. PMID:10506173
- ↑ Li J, Dong Y, Lu X, Wang L, Peng W, Zhang XC, Rao Z. Crystal structures and biochemical studies of human lysophosphatidic acid phosphatase type 6. Protein Cell. 2013 Jun 26. PMID:23807634 doi:10.1007/s13238-013-3031-z
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