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The structure of the first representative of Pfam family PF06475 reveals a new fold with possible involvement in glycolipid metabolism.

  • Author(s): Bakolitsa, Constantina
  • Kumar, Abhinav
  • McMullan, Daniel
  • Krishna, S Sri
  • Miller, Mitchell D
  • Carlton, Dennis
  • Najmanovich, Rafael
  • Abdubek, Polat
  • Astakhova, Tamara
  • Chiu, Hsiu Ju
  • Clayton, Thomas
  • Deller, Marc C
  • Duan, Lian
  • Elias, Ylva
  • Feuerhelm, Julie
  • Grant, Joanna C
  • Grzechnik, Slawomir K
  • Han, Gye Won
  • Jaroszewski, Lukasz
  • Jin, Kevin K
  • Klock, Heath E
  • Knuth, Mark W
  • Kozbial, Piotr
  • Marciano, David
  • Morse, Andrew T
  • Nigoghossian, Edward
  • Okach, Linda
  • Oommachen, Silvya
  • Paulsen, Jessica
  • Reyes, Ron
  • Rife, Christopher L
  • Trout, Christina V
  • van den Bedem, Henry
  • Weekes, Dana
  • White, Aprilfawn
  • Xu, Qingping
  • Hodgson, Keith O
  • Wooley, John
  • Elsliger, Marc André
  • Deacon, Ashley M
  • Godzik, Adam
  • Lesley, Scott A
  • Wilson, Ian A
  • et al.
Abstract

The crystal structure of PA1994 from Pseudomonas aeruginosa, a member of the Pfam PF06475 family classified as a domain of unknown function (DUF1089), reveals a novel fold comprising a 15-stranded β-sheet wrapped around a single α-helix that assembles into a tight dimeric arrangement. The remote structural similarity to lipoprotein localization factors, in addition to the presence of an acidic pocket that is conserved in DUF1089 homologs, phospholipid-binding and sugar-binding proteins, indicate a role for PA1994 and the DUF1089 family in glycolipid metabolism. Genome-context analysis lends further support to the involvement of this family of proteins in glycolipid metabolism and indicates possible activation of DUF1089 homologs under conditions of bacterial cell-wall stress or host-pathogen interactions.

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