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| | ==Crystal structure of a domain-swapped dimer of the second StARkin domain of Lam2== | | ==Crystal structure of a domain-swapped dimer of the second StARkin domain of Lam2== |
| - | <StructureSection load='5yqq' size='340' side='right' caption='[[5yqq]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='5yqq' size='340' side='right'caption='[[5yqq]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5yqq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YQQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YQQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5yqq]] is a 2 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=5YQQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YQQ FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YSP2, LAM2, LTC4, YDR326C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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]] 1.9Å</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=5yqq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yqq OCA], [http://pdbe.org/5yqq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yqq RCSB], [http://www.ebi.ac.uk/pdbsum/5yqq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yqq 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=5yqq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yqq OCA], [https://pdbe.org/5yqq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yqq RCSB], [https://www.ebi.ac.uk/pdbsum/5yqq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yqq ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/YSP2_YEAST YSP2_YEAST]] Involved in induction of programmed cell death in response to reactive oxygen species (ROS) (PubMed:16962064). May be involved in sterol transfer between intracellular membranes (PubMed:26001273).<ref>PMID:16962064</ref> <ref>PMID:26001273</ref> | + | [https://www.uniprot.org/uniprot/YSP2_YEAST YSP2_YEAST] Involved in induction of programmed cell death in response to reactive oxygen species (ROS) (PubMed:16962064). May be involved in sterol transfer between intracellular membranes (PubMed:26001273).<ref>PMID:16962064</ref> <ref>PMID:26001273</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Baker's yeast]] | + | [[Category: Large Structures]] |
| - | [[Category: Im, Y J]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Tong, J]] | + | [[Category: Im YJ]] |
| - | [[Category: Ligand binding domain]] | + | [[Category: Tong J]] |
| - | [[Category: Lipid transport]]
| + | |
| - | [[Category: Sterol]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| - | [[Category: Ysp2]]
| + | |
| Structural highlights
Function
YSP2_YEAST Involved in induction of programmed cell death in response to reactive oxygen species (ROS) (PubMed:16962064). May be involved in sterol transfer between intracellular membranes (PubMed:26001273).[1] [2]
Publication Abstract from PubMed
Membrane contact sites (MCSs) in eukaryotic cells are hotspots for lipid exchange, which is essential for many biological functions, including regulation of membrane properties and protein trafficking. Lipid transfer proteins anchored at membrane contact sites (LAMs) contain sterol-specific lipid transfer domains [StARkin domain (SD)] and multiple targeting modules to specific membrane organelles. Elucidating the structural mechanisms of targeting and ligand recognition by LAMs is important for understanding the interorganelle communication and exchange at MCSs. Here, we determined the crystal structures of the yeast Lam6 pleckstrin homology (PH)-like domain and the SDs of Lam2 and Lam4 in the apo form and in complex with ergosterol. The Lam6 PH-like domain displays a unique PH domain fold with a conserved N-terminal alpha-helix. The Lam6 PH-like domain lacks the basic surface for phosphoinositide binding, but contains hydrophobic patches on its surface, which are critical for targeting to endoplasmic reticulum (ER)-mitochondrial contacts. Structures of the LAM SDs display a helix-grip fold with a hydrophobic cavity and a flexible Omega1-loop as a lid. Ergosterol is bound to the pocket in a head-down orientation, with its hydrophobic acyl group located in the tunnel entrance. The Omega1-loop in an open conformation is essential for ergosterol binding by direct hydrophobic interaction. Structural comparison suggested that the sterol binding mode of the Lam2 SD2 is likely conserved among the sterol transfer proteins of the StARkin superfamily. Structural models of full-length Lam2 correlated with the sterol transport function at the membrane contact sites.
Structural basis of sterol recognition and nonvesicular transport by lipid transfer proteins anchored at membrane contact sites.,Tong J, Manik MK, Im YJ Proc Natl Acad Sci U S A. 2018 Jan 16. pii: 1719709115. doi:, 10.1073/pnas.1719709115. PMID:29339490[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sokolov S, Knorre D, Smirnova E, Markova O, Pozniakovsky A, Skulachev V, Severin F. Ysp2 mediates death of yeast induced by amiodarone or intracellular acidification. Biochim Biophys Acta. 2006 Sep-Oct;1757(9-10):1366-70. Epub 2006 Aug 2. PMID:16962064 doi:http://dx.doi.org/S0005-2728(06)00248-9
- ↑ Gatta AT, Wong LH, Sere YY, Calderon-Norena DM, Cockcroft S, Menon AK, Levine TP. A new family of StART domain proteins at membrane contact sites has a role in ER-PM sterol transport. Elife. 2015 May 22;4. doi: 10.7554/eLife.07253. PMID:26001273 doi:http://dx.doi.org/10.7554/eLife.07253
- ↑ Tong J, Manik MK, Im YJ. Structural basis of sterol recognition and nonvesicular transport by lipid transfer proteins anchored at membrane contact sites. Proc Natl Acad Sci U S A. 2018 Jan 16. pii: 1719709115. doi:, 10.1073/pnas.1719709115. PMID:29339490 doi:http://dx.doi.org/10.1073/pnas.1719709115
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