biostudies-literatureAlbesa-Jove DNIAID NIH HHSNINR NIH HHS10906https://www.ebi.ac.uk/biostudies/studies/S-EPMC4792965biostudies-literatureUnknown7The biosynthesis of phospholipids and glycolipids are critical pathways for virtually all cell membranes. PatA is an essential membrane associated acyltransferase involved in the biosynthesis of mycobacterial phosphatidyl-myo-inositol mannosides (PIMs). The enzyme transfers a palmitoyl moiety from palmitoyl-CoA to the 6-position of the mannose ring linked to 2-position of inositol in PIM1/PIM2. We report here the crystal structures of PatA from Mycobacterium smegmatis in the presence of its naturally occurring acyl donor palmitate and a nonhydrolyzable palmitoyl-CoA analog. The structures reveal an α/β architecture, with the acyl chain deeply buried into a hydrophobic pocket that runs perpendicular to a long groove where the active site is located. Enzyme catalysis is mediated by an unprecNature communicationsStructural basis for selective recognition of acyl chains by the membrane-associated acyltransferase PatA.PMC4792965R01 NR014846AI064798R01 AI064798Jackson MArrasate PGuerin MEEguskiza ASancho-Vaello ESvetlikova ZKordulakova JCifuente JOAlbesa-Jove DMikusova KBonnet PCarreras-Gonzalez AAngala SKTersa MfalseStructural basis for selective recognition of acyl chains by the membrane-associated acyltransferase PatA.The biosynthesis of phospholipids and glycolipids are critical pathways for virtually all cell membranes. PatA is an essential membrane associated acyltransferase involved in the biosynthesis of mycobacterial phosphatidyl-myo-inositol mannosides (PIMs). The enzyme transfers a palmitoyl moiety from palmitoyl-CoA to the 6-position of the mannose ring linked to 2-position of inositol in PIM1/PIM2. We report here the crystal structures of PatA from Mycobacterium smegmatis in the presence of its naturally occurring acyl donor palmitate and a nonhydrolyzable palmitoyl-CoA analog. The structures reveal an α/β architecture, with the acyl chain deeply buried into a hydrophobic pocket that runs perpendicular to a long groove where the active site is located. Enzyme catalysis is mediated by an unprec2016-01-01T00:00:00Z2016 Mar2026-05-01T22:03:53.571Z2025-06-01T03:55:46.122ZS-EPMC47929652696505710.1038/ncomms10906