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10.1038/nsmb.3436 http://scihub22266oqcxt.onion/10.1038/nsmb.3436 C5616210!5616210 !28714993     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28714993 &cmd=llinks): Failed to open stream: HTTP request failed! 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A two-helix motif positions the lysophosphatidic acid acyltransferase active site for catalysis within the membrane bilayer |pdf=|usr=}}{{28714993 }} gab.com Text A two-helix motif positions the lysophosphatidic acid acyltransferase active site for catalysis within the membrane bilayer JO: Nat Struct Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=28714993 #FOAvip Phosphatidic acid (PA), the central intermediate in membrane phospholipid synthesis, is generated by two acyltransferases in a pathway conserved in all life forms. The second step in this pathway is catalyzed by 1-acyl-sn-glycerol-3-phosphate acyltransferase, called PlsC in bacteria. Here we present the crystal structure of PlsC from Thermotoga maritima, revealing an unusual hydrophobic/aromatic N-terminal two-helix motif linked to an acyltransferase ??-domain that contains the catalytic HX(4)D motif. PlsC dictates the acyl chain composition of the 2-position of phospholipids, and the acyl chain selectivity 'ruler' is an appropriately placed and closed hydrophobic tunnel. We confirmed this by site-directed mutagenesis and membrane composition analysis of Escherichia coli cells that expressed mutant PlsC. Molecular dynamics (MD) simulations showed that the two-helix motif represents a novel substructure that firmly anchors the protein to one leaflet of the membrane. This binding mode allows the PlsC active site to acylate lysophospholipids within the membrane bilayer by using soluble acyl donors. Twit Text FOAVip A two-helix motif positions the lysophosphatidic acid acyltransferase active site for catalysis within the membrane bilayer ????Nat Struct Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=28714993 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28714993 #FOAvip English Wikipedia <ref>{{Cite pmid|28714993 }}</ref> A two-helix motif positions the lysophosphatidic acid acyltransferase active site for catalysis within the membrane bilayer #MMPMID28714993 Robertson RM ; Yao J ; Gajewski S ; Kumar G ; Martin EW ; Rock CO ; White SW Nat Struct Mol Biol 2017[Aug]; 24 (8 ): 666-671 PMID28714993 show ga Phosphatidic acid (PA), the central intermediate in membrane phospholipid synthesis, is generated by two acyltransferases in a pathway conserved in all life forms. The second step in this pathway is catalyzed by 1-acyl-sn-glycerol-3-phosphate acyltransferase, called PlsC in bacteria. Here we present the crystal structure of PlsC from Thermotoga maritima, revealing an unusual hydrophobic/aromatic N-terminal two-helix motif linked to an acyltransferase ??-domain that contains the catalytic HX(4)D motif. PlsC dictates the acyl chain composition of the 2-position of phospholipids, and the acyl chain selectivity 'ruler' is an appropriately placed and closed hydrophobic tunnel. We confirmed this by site-directed mutagenesis and membrane composition analysis of Escherichia coli cells that expressed mutant PlsC. Molecular dynamics (MD) simulations showed that the two-helix motif represents a novel substructure that firmly anchors the protein to one leaflet of the membrane. This binding mode allows the PlsC active site to acylate lysophospholipids within the membrane bilayer by using soluble acyl donors. |*Amino Acid Motifs [MESH] |*Lipid Bilayers [MESH] |Acyltransferases/*chemistry/genetics/*metabolism [MESH] |Catalysis [MESH] |Catalytic Domain [MESH] |Cell Membrane/enzymology [MESH] |Crystallography, X-Ray [MESH] |DNA Mutational Analysis [MESH] |Membrane Proteins/*chemistry/genetics/*metabolism [MESH] |Models, Molecular [MESH] |Molecular Dynamics Simulation [MESH] |Protein Conformation, alpha-Helical [MESH]A two-helix motif positions the lysophosphatidic acid acyltransferase (epmc).pdf DeepDyve Pubget Overpricing