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5d92

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'''Unreleased structure'''
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==Structure of a phosphatidylinositolphosphate (PIP) synthase from Renibacterium Salmoninarum==
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<StructureSection load='5d92' size='340' side='right' caption='[[5d92]], [[Resolution|resolution]] 3.62&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5d92]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D92 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D92 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=58A:5-O-[(R)-{[(S)-{(2R)-2,3-BIS[(9E)-OCTADEC-9-ENOYLOXY]PROPOXY}(HYDROXY)PHOSPHORYL]OXY}(HYDROXY)PHOSPHORYL]CYTIDINE'>58A</scene>, <scene name='pdbligand=8K6:OCTADECANE'>8K6</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5d91|5d91]]</td></tr>
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<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=5d92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d92 OCA], [http://pdbe.org/5d92 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d92 RCSB], [http://www.ebi.ac.uk/pdbsum/5d92 PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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The entry 5d92 is ON HOLD until Paper Publication
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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>
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Authors: Clarke, O.B., Tomasek, D.T., Jorge, C.D., Belcher Dufrisne, M., Kim, M., Banerjee, S., Rajashankar, K.R., Hendrickson, W.A., Santos, H., Mancia, F.
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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Description: Structure of a phosphatidylinositolphosphate (PIP) synthase from Renibacterium Salmoninarum
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<div class="pdbe-citations 5d92" style="background-color:#fffaf0;"></div>
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[[Category: Unreleased Structures]]
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== References ==
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[[Category: Rajashankar, K.R]]
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<references/>
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[[Category: Santos, H]]
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__TOC__
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[[Category: Tomasek, D.T]]
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</StructureSection>
[[Category: Banerjee, S]]
[[Category: Banerjee, S]]
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[[Category: Jorge, C.D]]
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[[Category: Clarke, O B]]
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[[Category: Clarke, O.B]]
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[[Category: Dufrisne, M Belcher]]
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[[Category: Hendrickson, W.A]]
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[[Category: Hendrickson, W A]]
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[[Category: Jorge, C D]]
[[Category: Kim, M]]
[[Category: Kim, M]]
[[Category: Mancia, F]]
[[Category: Mancia, F]]
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[[Category: Belcher Dufrisne, M]]
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[[Category: Rajashankar, K R]]
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[[Category: Santos, H]]
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[[Category: Tomasek, D T]]
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[[Category: Enzyme]]
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[[Category: Lipid biosynthesis]]
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[[Category: Membrane protein]]
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[[Category: Phosphatidylinositol]]

Revision as of 20:56, 30 November 2015

Structure of a phosphatidylinositolphosphate (PIP) synthase from Renibacterium Salmoninarum

5d92, resolution 3.62Å

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