Insights into ssDNA recognition by the OB fold from a structural and thermodynamic study of Sulfolobus SSB protein

ID Kerr, RIM Wadsworth, L Cubeddu, W Blankenfeldt, James Henderson Naismith, Malcolm Frederick White

Research output: Contribution to journalArticlepeer-review

99 Citations (Scopus)

Abstract

Information processing pathways such as DNA replication are conserved in eukaryotes and archaea and are significantly different from those found in bacteria. Single-stranded DNA-binding (SSB) proteins (or replication protein A, RPA, in eukaryotes) play a central role in many of these pathways. However, whilst euryarchaea have a eukaryotic-type RPA homologue, crenarchaeal SSB proteins appear much more similar to the bacterial proteins, with a single OB fold for DNA binding and a flexible C-terminal tail that is implicated in protein-protein interactions. We have determined the crystal structure of the SSB protein from the crenarchaeote Sulfolobus solfataricus to 1.26 Angstrom. The structure shows a striking and unexpected similarity to the DNA-binding domains of human RPA, providing confirmation of the close relationship between archaea and eukaryotes. The high resolution of the structure, together with thermodynamic and mutational studies of DNA binding, allow us to propose a molecular basis for DNA binding and define the features required for eukaryotic and archaeal OB folds.

Original languageEnglish
Pages (from-to)2561-2570
Number of pages10
JournalEMBO Journal
Volume22
Issue number11
DOIs
Publication statusPublished - 2 Jun 2003

Keywords

  • archaea
  • OB fold
  • protein structure
  • RPA
  • SSB protein
  • SINGLE-STRANDED-DNA
  • BINDING-PROTEIN
  • CRYSTAL-STRUCTURE
  • STRUCTURE REFINEMENT
  • DISTINCT COMPLEXES
  • REPLICATION
  • DOMAIN
  • SOLFATARICUS
  • RESOLUTION
  • MECHANISM

Fingerprint

Dive into the research topics of 'Insights into ssDNA recognition by the OB fold from a structural and thermodynamic study of Sulfolobus SSB protein'. Together they form a unique fingerprint.

Cite this