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

J Struct Funct Genomics. 2012 Sep;13(3):155-62. doi: 10.1007/s10969-012-9140-8. Epub 2012 Aug 3.

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).

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Amino Acid Motifs
  • Bacterial Proteins / chemistry*
  • Crystallography, X-Ray / methods*
  • DNA, Bacterial / chemistry
  • DNA-Binding Proteins / chemistry*
  • Magnetic Resonance Spectroscopy / methods*
  • Models, Genetic
  • Protein Conformation
  • Protein Folding
  • Protein Structure, Tertiary
  • Proteomics / methods*
  • Pseudomonas syringae / chemistry*
  • Pseudomonas syringae / genetics
  • Solutions / chemistry

Substances

  • Bacterial Proteins
  • DNA, Bacterial
  • DNA-Binding Proteins
  • Solutions