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10.1073/pnas.1719709115 http://scihub22266oqcxt.onion/10.1073/pnas.1719709115 C5798383!5798383 !29339490     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=29339490 &cmd=llinks): Failed to open stream: HTTP request failed! 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Structural basis of sterol recognition and nonvesicular transport by lipid transfer proteins anchored at membrane contact sites |pdf=|usr=}}{{29339490 }} gab.com Text Structural basis of sterol recognition and nonvesicular transport by lipid transfer proteins anchored at membrane contact sites JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=29339490 #FOAvip 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 ?-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 ?1-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 ?1-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. Twit Text FOAVip Structural basis of sterol recognition and nonvesicular transport by lipid transfer proteins anchored at membrane contact sites ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=29339490 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29339490 #FOAvip English Wikipedia <ref>{{Cite pmid|29339490 }}</ref> Structural basis of sterol recognition and nonvesicular transport by lipid transfer proteins anchored at membrane contact sites #MMPMID29339490 Tong J ; Manik MK ; Im YJ Proc Natl Acad Sci U S A 2018[Jan]; 115 (5 ): E856-E865 PMID29339490 show ga 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 ?-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 ?1-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 ?1-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. |Animals [MESH] |Binding Sites [MESH] |Biological Transport [MESH] |Carrier Proteins/*metabolism [MESH] |Cell Membrane/*metabolism [MESH] |Crystallography, X-Ray [MESH] |Endoplasmic Reticulum/metabolism [MESH] |Ergosterol/chemistry [MESH] |Escherichia coli/metabolism [MESH] |Green Fluorescent Proteins/metabolism [MESH] |Hydrophobic and Hydrophilic Interactions [MESH] |Ligands [MESH] |Lipids/chemistry [MESH] |Liposomes/chemistry [MESH] |Mice [MESH] |Mitochondria [MESH] |Mitochondrial Membranes/metabolism [MESH] |Pleckstrin Homology Domains [MESH] |Protein Binding [MESH] |Protein Domains [MESH] |Protein Structure, Secondary [MESH] |Sterols/*chemistry [MESH]Structural basis of sterol recognition and nonvesicular transport by l(epmc).pdf DeepDyve Pubget Overpricing