5d91: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5d91]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus_DSM_4304 Archaeoglobus fulgidus DSM 4304] and [https://en.wikipedia.org/wiki/Renibacterium_salmoninarum_ATCC_33209 Renibacterium salmoninarum ATCC 33209]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D91 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D91 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5d91]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus_DSM_4304 Archaeoglobus fulgidus DSM 4304] and [https://en.wikipedia.org/wiki/Renibacterium_salmoninarum_ATCC_33209 Renibacterium salmoninarum ATCC 33209]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D91 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D91 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=8K6:OCTADECANE'>8K6</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.501Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=8K6:OCTADECANE'>8K6</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5d91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d91 OCA], [https://pdbe.org/5d91 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d91 RCSB], [https://www.ebi.ac.uk/pdbsum/5d91 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d91 ProSAT]</span></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=5d91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d91 OCA], [https://pdbe.org/5d91 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d91 RCSB], [https://www.ebi.ac.uk/pdbsum/5d91 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d91 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 11:44, 27 September 2023
Structure of a phosphatidylinositolphosphate (PIP) synthase from Renibacterium SalmoninarumStructure of a phosphatidylinositolphosphate (PIP) synthase from Renibacterium Salmoninarum
Structural highlights
FunctionO27985_ARCFU A9WSF5_RENSM Catalyzes the conjugation of the 1'-hydroxyl group of D-myo-inositol-3-phosphate (also named L-myo-inositol-1-phosphate) with a lipid tail of cytidine diphosphate diacylglycerol (CDP-DAG), forming phosphatidylinositol phosphate (PIP) and CMP. PIP is a precursor of phosphatidylinositol (PI) which is an essential lipid required for cell wall formation.[HAMAP-Rule:MF_02241] Publication Abstract from PubMedPhosphatidylinositol is critical for intracellular signalling and anchoring of carbohydrates and proteins to outer cellular membranes. The defining step in phosphatidylinositol biosynthesis is catalysed by CDP-alcohol phosphotransferases, transmembrane enzymes that use CDP-diacylglycerol as donor substrate for this reaction, and either inositol in eukaryotes or inositol phosphate in prokaryotes as the acceptor alcohol. Here we report the structures of a related enzyme, the phosphatidylinositol-phosphate synthase from Renibacterium salmoninarum, with and without bound CDP-diacylglycerol to 3.6 and 2.5 A resolution, respectively. These structures reveal the location of the acceptor site, and the molecular determinants of substrate specificity and catalysis. Functional characterization of the 40%-identical ortholog from Mycobacterium tuberculosis, a potential target for the development of novel anti-tuberculosis drugs, supports the proposed mechanism of substrate binding and catalysis. This work therefore provides a structural and functional framework to understand the mechanism of phosphatidylinositol-phosphate biosynthesis. Structural basis for phosphatidylinositol-phosphate biosynthesis.,Clarke OB, Tomasek D, Jorge CD, Dufrisne MB, Kim M, Banerjee S, Rajashankar KR, Shapiro L, Hendrickson WA, Santos H, Mancia F Nat Commun. 2015 Oct 16;6:8505. doi: 10.1038/ncomms9505. PMID:26510127[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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