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

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Oct 1;66(Pt 10):1218-25. doi: 10.1107/S1744309109050416. Epub 2010 Mar 5.

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Crystallography, X-Ray
  • Genome, Bacterial
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Folding*
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Rhodobacteraceae / chemistry*
  • Rhodobacteraceae / genetics
  • Rhodobacteraceae / metabolism
  • Shewanella / chemistry*
  • Shewanella / genetics
  • Shewanella / metabolism
  • Signal Transduction*
  • Structural Homology, Protein

Substances

  • Bacterial Proteins

Associated data

  • PDB/2RA9
  • PDB/2RE3