5d91: Difference between revisions
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==Structure of a phosphatidylinositolphosphate (PIP) synthase from Renibacterium Salmoninarum== | |||
<StructureSection load='5d91' size='340' side='right' caption='[[5d91]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5d91]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arcfu Arcfu]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D91 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5d92|5d92]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RSal33209_2010 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224325 ARCFU])</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=5d91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d91 OCA], [http://pdbe.org/5d91 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d91 RCSB], [http://www.ebi.ac.uk/pdbsum/5d91 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5d91 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Phosphatidylinositol 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<ref>PMID:26510127</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5d91" style="background-color:#fffaf0;"></div> | |||
== References == | |||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Arcfu]] | |||
[[Category: Banerjee, S]] | [[Category: Banerjee, S]] | ||
[[Category: | [[Category: Clarke, O B]] | ||
[[Category: | [[Category: Dufrisne, M Belcher]] | ||
[[Category: Hendrickson, W | [[Category: Hendrickson, W A]] | ||
[[Category: Jorge, C D]] | |||
[[Category: Kim, M]] | [[Category: Kim, M]] | ||
[[Category: Mancia, F]] | [[Category: Mancia, F]] | ||
[[Category: | [[Category: Rajashankar, K R]] | ||
[[Category: Santos, H]] | |||
[[Category: Tomasek, D T]] | |||
[[Category: Enzyme]] | |||
[[Category: Lipid biosynthesis]] | |||
[[Category: Membrane protein]] | |||
[[Category: Phosphatidylinositol]] | |||
Revision as of 17:05, 16 November 2017
Structure of a phosphatidylinositolphosphate (PIP) synthase from Renibacterium SalmoninarumStructure of a phosphatidylinositolphosphate (PIP) synthase from Renibacterium Salmoninarum
Structural highlights
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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