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The structure of Jann_2411 (DUF1470) from Jannaschia sp. at 1.45 Å resolution reveals a new fold (the ABATE domain) and suggests its possible role as a transcription regulator.

  • Author(s): Bakolitsa, Constantina
  • Bateman, Alex
  • Jin, Kevin K
  • McMullan, Daniel
  • Krishna, S Sri
  • Miller, Mitchell D
  • Abdubek, Polat
  • Acosta, Claire
  • Astakhova, Tamara
  • Axelrod, Herbert L
  • Burra, Prasad
  • Carlton, Dennis
  • Chiu, Hsiu Ju
  • Clayton, Thomas
  • Das, Debanu
  • Deller, Marc C
  • Duan, Lian
  • Elias, Ylva
  • Feuerhelm, Julie
  • Grant, Joanna C
  • Grzechnik, Anna
  • Grzechnik, Slawomir K
  • Han, Gye Won
  • Jaroszewski, Lukasz
  • Klock, Heath E
  • Knuth, Mark W
  • Kozbial, Piotr
  • Kumar, Abhinav
  • Marciano, David
  • Morse, Andrew T
  • Murphy, Kevin D
  • Nigoghossian, Edward
  • Okach, Linda
  • Oommachen, Silvya
  • Paulsen, Jessica
  • Reyes, Ron
  • Rife, Christopher L
  • Sefcovic, Natasha
  • Tien, Henry
  • Trame, Christine B
  • 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
  • Wilson, Ian A
  • et al.
Abstract

The crystal structure of Jann_2411 from Jannaschia sp. strain CCS1, a member of the Pfam PF07336 family classified as a domain of unknown function (DUF1470), was solved to a resolution of 1.45 Å by multiple-wavelength anomalous dispersion (MAD). This protein is the first structural representative of the DUF1470 Pfam family. Structural analysis revealed a two-domain organization, with the N-terminal domain presenting a new fold called the ABATE domain that may bind an as yet unknown ligand. The C-terminal domain forms a treble-clef zinc finger that is likely to be involved in DNA binding. Analysis of the Jann_2411 protein and the broader ABATE-domain family suggests a role as stress-induced transcriptional regulators.

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