5F2T

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

5F2T の概要

• エントリーDOI: 10.2210/pdb5f2t/pdb
• 分子名称: Phosphatidylinositol mannoside acyltransferase, PALMITIC ACID, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: acyltransferase, glycolipid biosynthesis, transferase
• 由来する生物種: Mycobacterium smegmatis
• 細胞内の位置: Cell membrane ; Single-pass membrane protein : A0QWG5
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 69134.66

構造登録者

Albesa-Jove, D.,Svetlikova, Z.,Carreras-Gonzalez, A.,Tersa, M.,Sancho-Vaello, E.,Cifuente, J.O.,Mikusova, K.,Guerin, M.E. (登録日: 2015-12-02, 公開日: 2016-03-09, 最終更新日: 2024-05-08)

主引用文献

Albesa-Jove, D.,Svetlikova, Z.,Tersa, M.,Sancho-Vaello, E.,Carreras-Gonzalez, A.,Bonnet, P.,Arrasate, P.,Eguskiza, A.,Angala, S.K.,Cifuente, J.O.,Kordulakova, J.,Jackson, M.,Mikusova, K.,Guerin, M.E.
Structural basis for selective recognition of acyl chains by the membrane-associated acyltransferase PatA.
Nat Commun, 7:10906-10906, 2016

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 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.

PubMed: 26965057
DOI: 10.1038/ncomms10906

実験手法

X-RAY DIFFRACTION (2.06 Å)