Chemical shift assignments of the homodimer protein SP_0782 (7-79) from Streptococcus pneumoniae

Biomol NMR Assign. 2016 Oct;10(2):341-4. doi: 10.1007/s12104-016-9697-4. Epub 2016 Jul 7.

Abstract

The protein SP_0782 from Streptococcus pneumonia is a small homodimeric protein that belongs to a protein family containing representative members with single-stranded DNA (ssDNA) binding functions. The ssDNA binding of the homolog YdbC from Lactococcus lactis was previously characterized when bound to a 20-mer of pyridine-rich ssDNA, sharing an overall similar structural fold with the human transcription coactivator PC4. We report that SP_0782 exhibits distinct differences in ssDNA binding properties from YdbC as revealed by NMR titration experiments. Unlike the binding of the ssDNA dT19G1 to PC4 and YdbC, SP_0782 resulted in aggregation. In addition, SP_0782 exhibits favorable binding to shorter ssDNA such as dT6. The reason is unclear, and the SP_0782 structure-function relationship remains to be elucidated. Here, we report the complete (1)H, (13)C, and (15)N backbone and side chain NMR assignments of SP_0782, residues 7-79.

Keywords: Assignment; NMR spectroscopy; SP_0782; ssDNA binding.

Publication types

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

MeSH terms

  • Bacterial Proteins / chemistry*
  • Nuclear Magnetic Resonance, Biomolecular*
  • Protein Multimerization*
  • Protein Structure, Quaternary
  • Streptococcus pneumoniae*

Substances

  • Bacterial Proteins