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Structures of the first representatives of Pfam family PF06938 (DUF1285) reveal a new fold with repeated structural motifs and possible involvement in signal transduction.

  • Author(s): Han, Gye Won
  • Bakolitsa, Constantina
  • Miller, Mitchell D
  • Kumar, Abhinav
  • Carlton, Dennis
  • Najmanovich, Rafael J
  • Abdubek, Polat
  • Astakhova, Tamara
  • Axelrod, Herbert L
  • Chen, Connie
  • Chiu, Hsiu Ju
  • Clayton, Thomas
  • Das, Debanu
  • Deller, Marc C
  • Duan, Lian
  • Ernst, Dustin
  • Feuerhelm, Julie
  • Grant, Joanna C
  • Grzechnik, Anna
  • Jaroszewski, Lukasz
  • Jin, Kevin K
  • Johnson, Hope A
  • Klock, Heath E
  • Knuth, Mark W
  • Kozbial, Piotr
  • Krishna, S Sri
  • Marciano, David
  • McMullan, Daniel
  • Morse, Andrew T
  • Nigoghossian, Edward
  • Okach, Linda
  • Reyes, Ron
  • Rife, Christopher L
  • Sefcovic, Natasha
  • Tien, Henry J
  • Trame, Christine B
  • 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 crystal structures of SPO0140 and Sbal_2486 were determined using the semiautomated high-throughput pipeline of the Joint Center for Structural Genomics (JCSG) as part of the NIGMS Protein Structure Initiative (PSI). The structures revealed a conserved core with domain duplication and a superficial similarity of the C-terminal domain to pleckstrin homology-like folds. The conservation of the domain interface indicates a potential binding site that is likely to involve a nucleotide-based ligand, with genome-context and gene-fusion analyses additionally supporting a role for this family in signal transduction, possibly during oxidative stress.

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