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Structural basis for selective recognition of acyl chains by the membrane-associated acyltransferase PatA.

Nat Commun. 2016; 
Albesa-JovéDavid,SvetlíkováZuzana,TersaMontse,Sancho-VaelloEnea,Carreras-GonzálezAna,BonnetPascal,ArrasatePedro,EguskizaAnder,AngalaShiva K,CifuenteJavier O,KordulákováJana,JacksonMary,MikušováKatarína,GuerinMarce
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Custom Vector Construction The PatA-H126A, PatA-D131A, PatA-E149A, PatA-R164A, PatA-E200A and PatA-H284A mutants, and double mutant PatA-F182W/L197W were synthetized by GenScript using the pJAM2-patA construct, and further expressed and purified to apparent homogeneity as described for the recombinant PatA enzyme. Get A Quote

摘要

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 lon... More

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