5f31

Crystal structure of membrane associated PatA from Mycobacterium smegmatis in complex with palmitate - P 42 21 2 space group

spinqualitylabelsall models 5f31, resolution 2.43Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5f31 is a 1 chain structure with sequence from Mycolicibacterium smegmatis MC2 155. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.43Å Ligands: EOH, NA, PLM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ACYLT_MYCS2 Catalyzes the acylation to the position 6 of the alpha-1,2-linked mannose residue of the phosphatidyl-myo-inositol dimannoside (PIM2) or monomannoside (PIM1). Publication Abstract from PubMed 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 alpha/beta 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 unprecedented charge relay system, which markedly diverges from the canonical HX4D motif. Our studies establish the mechanistic basis of substrate/membrane recognition and catalysis for an important family of acyltransferases, providing exciting possibilities for inhibitor design. Structural basis for selective recognition of acyl chains by the membrane-associated acyltransferase PatA.,Albesa-Jove D, Svetlikova Z, Tersa M, Sancho-Vaello E, Carreras-Gonzalez A, Bonnet P, Arrasate P, Eguskiza A, Angala SK, Cifuente JO, Kordulakova J, Jackson M, Mikusova K, Guerin ME Nat Commun. 2016 Mar 11;7:10906. doi: 10.1038/ncomms10906. PMID:26965057 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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