Solution NMR and X-ray crystal structures of Pseudomonas syringae Pspto-3016 from protein domain family PF04237 (DUF419) adopt a "double wing" DNA binding motif

Erik A. Feldmann, Jayaraman Seetharaman, Theresa A. Ramelot, Scott Lew, Li Zhao, Keith Hamilton, Colleen Ciccosanti, Rong Xiao, Thomas B. Acton, John K. Everett, Liang Tong, Gaetano T. Montelione, Michael A. Kennedy

Research output: Contribution to journalArticlepeer-review

5 Scopus citations

Abstract

The protein Pspto-3016 is a 117-residue member of the protein domain family PF04237 (DUF419), which is to date a functionally uncharacterized family of proteins. In this report, we describe the structure of Pspto-3016 from Pseudomonas syringae solved by both solution NMR and X-ray crystallography at 2.5 Å resolution. In both cases, the structure of Pspto-3016 adopts a "double wing" α/β sandwich fold similar to that of protein YjbR from Escherichia coli and to the C-terminal DNA binding domain of the MotA transcription factor (MotCF) from T4 bacteriophage, along with other uncharacterized proteins. Pspto-3016 was selected by the Protein Structure Initiative of the National Institutes of Health and the Northeast Structural Genomics Consortium (NESG ID PsR293).

Original languageEnglish (US)
Pages (from-to)155-162
Number of pages8
JournalJournal of Structural and Functional Genomics
Volume13
Issue number3
DOIs
StatePublished - Sep 2012

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry
  • Genetics

Keywords

  • 2KFP
  • 3H9X
  • DUF419
  • Double wing
  • NMR
  • PF04237
  • Pspto-3016
  • Structural genomics
  • X-ray crystallography

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