Crystal structure of the hyperthermophilic archaeal DNA-binding protein Sso10b2 at a resolution of 1.85 Angstroms

Chia Cheng Chou, Ting Wan Lin, Chin Yu Chen, Andrew H.J. Wang

Research output: Contribution to journalArticlepeer-review

46 Citations (Scopus)

Abstract

The crystal structure of a small, basic DNA binding protein, Sso10b2, from the thermoacidophilic archaeon ]Sulfolobus solfataricus was determined by the Zn multiwavelength anomalous diffraction method and refined to 1.85 Å resolution. The 89-amino-acid protein adopts a βαβαββ topology. The structure is similar to that of Sso10b1 (also called Alba) from the same organism. However, Sso10b2 contains an arginine-rich loop RDRRR motif, which may play an important role in nucleic acid binding. There are two independent Sso10b2 proteins in the asymmetric unit, and a plausible stable dimer could be deduced from the crystal structure. Topology comparison revealed that Sso10b2 is similar to several RNA-binding proteins, including IF3-C, YhhP, and DNase I. Models of the Sso10b2 dimer bound to either B-DNA or A-DNA have been constructed.

Original languageEnglish
Pages (from-to)4066-4073
Number of pages8
JournalJournal of Bacteriology
Volume185
Issue number14
DOIs
Publication statusPublished - Jul 2003
Externally publishedYes

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

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