{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Albesa-Jove D"],"funding":["NIAID NIH HHS","NINR NIH HHS"],"pagination":["10906"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4792965"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["7"],"pubmed_abstract":["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 unprec"],"journal":["Nature communications"],"pubmed_title":["Structural basis for selective recognition of acyl chains by the membrane-associated acyltransferase PatA."],"pmcid":["PMC4792965"],"funding_grant_id":["R01 NR014846","AI064798","R01 AI064798"],"pubmed_authors":["Jackson M","Arrasate P","Guerin ME","Eguskiza A","Sancho-Vaello E","Svetlikova Z","Kordulakova J","Cifuente JO","Albesa-Jove D","Mikusova K","Bonnet P","Carreras-Gonzalez A","Angala SK","Tersa M"],"additional_accession":[]},"is_claimable":false,"name":"Structural basis for selective recognition of acyl chains by the membrane-associated acyltransferase PatA.","description":"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 unprec","dates":{"release":"2016-01-01T00:00:00Z","publication":"2016 Mar","modification":"2026-05-01T22:03:53.571Z","creation":"2025-06-01T03:55:46.122Z"},"accession":"S-EPMC4792965","cross_references":{"pubmed":["26965057"],"doi":["10.1038/ncomms10906"]}}