6bje

Crystal Structure of Lysophospholipase A2 Conjugated with Phenylmethylsulfonyl Fluoride

spinqualitylabelsall models 6bje, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6bje is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.7Å Ligands: PMS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function LYPA2_HUMAN May hydrolyze fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS. Has lysophospholipase activity (By similarity). Deacylates GAP43. Publication Abstract from PubMed Lysophospholipids (LysoPLs) are bioactive lipid species involved in cellular signaling processes and the regulation of cell membrane structure. LysoPLs are metabolized through the action of lysophospholipases, including lysophospholipase A1 (LYPLA1) and lysophospholipase A2 (LYPLA2). A new X-ray crystal structure of LYPLA2 compared with a previously published structure of LYPLA1 demonstrated near-identical folding of the two enzymes; however, LYPLA1 and LYPLA2 have displayed distinct substrate specificities in recombinant enzyme assays. To determine how these in vitro substrate preferences translate into a relevant cellular setting and better understand the enzymes' role in LysoPL metabolism, CRISPR-Cas9 technology was utilized to generate stable KOs of Lypla1 and/or Lypla2 in Neuro2a cells. Using these cellular models in combination with a targeted lipidomics approach, LysoPL levels were quantified and compared between cell lines to determine the effect of losing lysophospholipase activity on lipid metabolism. This work suggests that LYPLA1 and LYPLA2 are each able to account for the loss of the other to maintain lipid homeostasis in cells; however, when both are deleted, LysoPL levels are dramatically increased, causing phenotypic and morphological changes to the cells. Lysophospholipases cooperate to mediate lipid homeostasis and lysophospholipid signaling.,Wepy JA, Galligan JJ, Kingsley PJ, Xu S, Goodman MC, Tallman KA, Rouzer CA, Marnett LJ J Lipid Res. 2019 Feb;60(2):360-374. doi: 10.1194/jlr.M087890. Epub 2018 Nov 27. PMID:30482805 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Thioesterase 3D structures

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