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10.1126/science.1246774 http://scihub22266oqcxt.onion/10.1126/science.1246774 C4390396!4390396!24558159     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Science 2014 ; 343 (6173): 878-81 Nephropedia Template TP {{tp|p=24558159|t=2014. Structural insights into ubiquinone biosynthesis in membranes |pdf=|usr=}}{{24558159}} gab.com Text Structural insights into ubiquinone biosynthesis in membranes JO: Science http://www.kidney.de/pget.php?&tw=1&pmid=24558159 #FOAvip Biosynthesis of ubiquinones requires the intramembrane UbiA enzyme, an archetypal member of a superfamily of prenyltransferases that generates lipophilic aromatic compounds. Mutations in eukaryotic superfamily members have been linked to cardiovascular degeneration and Parkinson's disease. To understand how quinones are produced within membranes, we report the crystal structures of an archaeal UbiA in its apo and substrate-bound states at 3.3 and 3.6Å resolution, respectively. The structures reveal nine transmembrane helices and an extra-membrane cap domain that surround a large central cavity containing the active site. To facilitate the catalysis inside membranes, UbiA has an unusual active site that opens laterally to the lipid bilayer. Our studies illuminate general mechanisms for substrate recognition and catalysis in the UbiA superfamily and rationalize disease-related mutations in humans. Twit Text FOAVip Structural insights into ubiquinone biosynthesis in membranes ????Science http://www.kidney.de/pget.php?&tw=1&pmid=24558159 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24558159 #FOAvip English Wikipedia <ref>{{Cite pmid|24558159}}</ref> Structural insights into ubiquinone biosynthesis in membranes #MMPMID24558159 Cheng W; Li W Science 2014[Feb]; 343 (6173): 878-81 PMID24558159show ga Biosynthesis of ubiquinones requires the intramembrane UbiA enzyme, an archetypal member of a superfamily of prenyltransferases that generates lipophilic aromatic compounds. Mutations in eukaryotic superfamily members have been linked to cardiovascular degeneration and Parkinson's disease. To understand how quinones are produced within membranes, we report the crystal structures of an archaeal UbiA in its apo and substrate-bound states at 3.3 and 3.6Å resolution, respectively. The structures reveal nine transmembrane helices and an extra-membrane cap domain that surround a large central cavity containing the active site. To facilitate the catalysis inside membranes, UbiA has an unusual active site that opens laterally to the lipid bilayer. Our studies illuminate general mechanisms for substrate recognition and catalysis in the UbiA superfamily and rationalize disease-related mutations in humans. äStructural insights into ubiquinone biosynthesis in membranes (epmc).pdf DeepDyve Pubget Overpricing