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

نویسندگان

  • Constantina Bakolitsa
  • Alex Bateman
  • Kevin K. Jin
  • Daniel McMullan
  • S. Sri Krishna
  • Mitchell D. Miller
  • Polat Abdubek
  • Claire Acosta
  • Tamara Astakhova
  • Herbert L. Axelrod
  • Prasad Burra
  • Dennis Carlton
  • Hsiu-Ju Chiu
  • Thomas Clayton
  • Debanu Das
  • Marc C. Deller
  • Lian Duan
  • Ylva Elias
  • Julie Feuerhelm
  • Joanna C. Grant
  • Anna Grzechnik
  • Slawomir K. Grzechnik
  • Gye Won Han
  • Lukasz Jaroszewski
  • Heath E. Klock
  • Mark W. Knuth
  • Piotr Kozbial
  • Abhinav Kumar
  • David Marciano
  • Andrew T. Morse
  • Kevin D. Murphy
  • Edward Nigoghossian
  • Linda Okach
  • Silvya Oommachen
  • Jessica Paulsen
  • Ron Reyes
  • Christopher L. Rife
  • Natasha Sefcovic
  • Henry Tien
  • Christine B. Trame
  • Christina V. Trout
  • Henry van den Bedem
  • Dana Weekes
  • Aprilfawn White
  • Qingping Xu
  • Keith O. Hodgson
  • John Wooley
  • Marc-André Elsliger
  • Ashley M. Deacon
  • Adam Godzik
  • Scott Lesley
  • Ian A. Wilson
چکیده

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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عنوان ژورنال:

دوره 66  شماره 

صفحات  -

تاریخ انتشار 2010