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

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 A resolution. The 89-amino-acid protein adopts a betaalphabetaalphabetabeta 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.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Chou CC,Lin TW,Chen CY,Wang AH

doi

10.1128/jb.185.14.4066-4073.2003

keywords:

subject

Has Abstract

pub_date

2003-07-01 00:00:00

pages

4066-73

issue

14

eissn

0021-9193

issn

1098-5530

journal_volume

185

pub_type

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