7zgb
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7zgb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ZGB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ZGB FirstGlance]. <br> | <table><tr><td colspan='2'>[[7zgb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ZGB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ZGB FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IUJ:4-fluoranyl-~{N}-[(4-pyrrolidin-1-ylphenyl)methyl]benzamide'>IUJ</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]] 2.7Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IUJ:4-fluoranyl-~{N}-[(4-pyrrolidin-1-ylphenyl)methyl]benzamide'>IUJ</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=7zgb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7zgb OCA], [https://pdbe.org/7zgb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7zgb RCSB], [https://www.ebi.ac.uk/pdbsum/7zgb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7zgb 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=7zgb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7zgb OCA], [https://pdbe.org/7zgb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7zgb RCSB], [https://www.ebi.ac.uk/pdbsum/7zgb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7zgb ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/SEC14_YEAST SEC14_YEAST] Required for transport of secretory proteins from the Golgi complex. Catalyzes the transfer of phosphatidylinositol and phosphatidylcholine between membranes in vitro. Essential for viability and secretion. | [https://www.uniprot.org/uniprot/SEC14_YEAST SEC14_YEAST] Required for transport of secretory proteins from the Golgi complex. Catalyzes the transfer of phosphatidylinositol and phosphatidylcholine between membranes in vitro. Essential for viability and secretion. | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Phosphatidylinositol (PtdIns) transfer proteins (PITPs) enhance the activities of PtdIns 4-OH kinases that generate signaling pools of PtdIns-4-phosphate. In that capacity, PITPs serve as key regulators of lipid signaling in eukaryotic cells. Although the PITP phospholipid exchange cycle is the engine that stimulates PtdIns 4-OH kinase activities, the underlying mechanism is not understood. Herein, we apply an integrative structural biology approach to investigate interactions of the yeast PITP Sec14 with small-molecule inhibitors (SMIs) of its phospholipid exchange cycle. Using a combination of X-ray crystallography, solution NMR spectroscopy, and atomistic MD simulations, we dissect how SMIs compete with native Sec14 phospholipid ligands and arrest phospholipid exchange. Moreover, as Sec14 PITPs represent new targets for the development of next-generation antifungal drugs, the structures of Sec14 bound to SMIs of diverse chemotypes reported in this study will provide critical information required for future structure-based design of next-generation lead compounds directed against Sec14 PITPs of virulent fungi. | ||
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| - | Mechanisms by Which Small Molecules of Diverse Chemotypes Arrest Sec14 Lipid Transfer Activity.,Chen XR, Poudel L, Hong Z, Johnen P, Katti S, Tripathi A, Nile AH, Green SM, Khan D, Schaaf G, Bono F, Bankaitis VA, Igumenova TI J Biol Chem. 2023 Jan 2:102861. doi: 10.1016/j.jbc.2022.102861. PMID:36603766<ref>PMID:36603766</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 7zgb" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Structure of yeast Sec14p with NPPM112
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