Biomolecular NMR Assignments

, Volume 10, Issue 2, pp 341–344 | Cite as

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

Article

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 1H, 13C, and 15N backbone and side chain NMR assignments of SP_0782, residues 7–79.

Keywords

SP_0782 ssDNA binding NMR spectroscopy Assignment 

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Copyright information

© Springer Science+Business Media Dordrecht 2016

Authors and Affiliations

  1. 1.State Key Laboratory of Magnetic Resonance and Atomic Molecular Physics, National Center for Magnetic Resonance in Wuhan, Wuhan Institute of Physics and MathematicsChinese Academy of SciencesWuhanChina
  2. 2.Department of Chemistry and Biochemistry, and the Northeast Structural Genomics ConsortiumMiami UniversityOxfordUSA

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