Patatin-like phospholipase domain QuickView

Description:: The patatin glycoprotein is a nonspecific lipid acyl hydrolase that is foundin high concentrations in mature potato tubers. Patatin is reported to play arole in plant signaling, to cleave fatty acids from membrane lipids, and toact as defense against plant parasites. Proteins encoding a patatin-likephospholipase (PNPLA) domain are ubiquitously distributed across all lifeforms, including eukaryotes and prokaryotes, and are observed to participatein a miscellany of biological roles, including sepsis induction, hostcolonization, triglyceride metabolism, and membrane trafficking. PNPLA domaincontaining proteins display lipase and transacylase properties and appear tohave major roles in lipid and energy homeostasis.The ~180-amino acid PNPLA domain harbors the evolutionarily conservedconsensus serine lipase motif Gly-X-Ser-X-Gly.It displays an alpha/beta classprotein fold with approximately three layers, basically alpha/beta/alpha incontent, in which a central six-stranded beta-sheet is sandwiched essentiallybetween alpha-helices front and back. The central beta-sheetcontains five parallel strands and an antiparallel strand at the edge of thesheet. The PNPLA domain has a Ser-Asp catalytic dyad. The catalytic Serresides in a sharp nucleophile elbow turn loop which follows a beta-strand(beta5) of the central beta-sheet and precedes a helix (helix C).

QuickView for Patatin-like phospholipase domain (biogroup)