5jwy
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of lipid phosphate phosphatase PgpB complex with PE== | |
| - | + | <StructureSection load='5jwy' size='340' side='right' caption='[[5jwy]], [[Resolution|resolution]] 3.20Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5jwy]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JWY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JWY FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=46E:(2R)-3-{[(S)-(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-2-(TETRADECANOYLOXY)PROPYL+TETRADECANOATE'>46E</scene></td></tr> | |
| - | [[Category: | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=5jwy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jwy OCA], [http://pdbe.org/5jwy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jwy RCSB], [http://www.ebi.ac.uk/pdbsum/5jwy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jwy ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/PGPB_ECOLI PGPB_ECOLI]] Catalyzes the dephosphorylation of diacylglycerol diphosphate (DGPP) to phosphatidate (PA) and the subsequent dephosphorylation of PA to diacylglycerol (DAG). Also has undecaprenyl pyrophosphate phosphatase activity, required for the biosynthesis of the lipid carrier undecaprenyl phosphate. Can also use lysophosphatidic acid (LPA) and phosphatidylglycerophosphate as substrates. The pattern of activities varies according to subcellular location, PGP phosphatase activity is higher in the cytoplasmic membrane, whereas PA and LPA phosphatase activities are higher in the outer membrane. Activity is independent of a divalent cation ion and insensitive to inhibition by N-ethylmaleimide.<ref>PMID:15778224</ref> <ref>PMID:18411271</ref> <ref>PMID:21148555</ref> <ref>PMID:8940025</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Tong, S]] | ||
| + | [[Category: Wang, M]] | ||
| + | [[Category: Zheng, L]] | ||
| + | [[Category: Enzyme]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Protein-lipid complex]] | ||
| + | [[Category: Transmembrane helice]] | ||
Revision as of 15:37, 26 July 2016
Structure of lipid phosphate phosphatase PgpB complex with PE
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