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Structure of the first representative of Pfam family PF09410 (DUF2006) reveals a structural signature of the calycin superfamily that suggests a role in lipid metabolism.

  • Author(s): Chiu, Hsiu Ju
  • Bakolitsa, Constantina
  • Skerra, Arne
  • Lomize, Andrei
  • Carlton, Dennis
  • Miller, Mitchell D
  • Krishna, S Sri
  • Abdubek, Polat
  • Astakhova, Tamara
  • Axelrod, Herbert L
  • Clayton, Thomas
  • Deller, Marc C
  • Duan, Lian
  • Feuerhelm, Julie
  • Grant, Joanna C
  • Grzechnik, Slawomir K
  • Han, Gye Won
  • Jaroszewski, Lukasz
  • Jin, Kevin K
  • Klock, Heath E
  • Knuth, Mark W
  • Kozbial, Piotr
  • Kumar, Abhinav
  • Marciano, David
  • McMullan, Daniel
  • Morse, Andrew T
  • Nigoghossian, Edward
  • Okach, Linda
  • Paulsen, Jessica
  • Reyes, Ron
  • Rife, Christopher L
  • van den Bedem, Henry
  • Weekes, Dana
  • 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 first structural representative of the domain of unknown function DUF2006 family, also known as Pfam family PF09410, comprises a lipocalin-like fold with domain duplication. The finding of the calycin signature in the N-terminal domain, combined with remote sequence similarity to two other protein families (PF07143 and PF08622) implicated in isoprenoid metabolism and the oxidative stress response, support an involvement in lipid metabolism. Clusters of conserved residues that interact with ligand mimetics suggest that the binding and regulation sites map to the N-terminal domain and to the interdomain interface, respectively.

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