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Journal of Bacteriology, July 2003, p. 4066-4073, Vol. 185, No. 14
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.14.4066-4073.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Crystal Structure of the Hyperthermophilic Archaeal DNA-Binding Protein Sso10b2 at a Resolution of 1.85 Angstroms

Chia-Cheng Chou,1,2 Ting-Wan Lin,1 Chin-Yu Chen,3 and Andrew H.-J. Wang1,2*

Institute of Biological Chemistry,1 Core Facility for Protein X-Ray Crystallography, Academia Sinica,2 Institute of Chemistry, National Taiwan University, Taipei, Taiwan3

Received 21 February 2003/ Accepted 23 April 2003

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 ß{alpha}ß{alpha}ßß 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.

* Corresponding author. Mailing address: Core Facility for Protein X-Ray Crystallography, Academia Sinica, Taipei 115, Taiwan. Phone: 886 2 27855696, ext. 1010. Fax: 886 2 27882043. E-mail: ahjwang{at}gate.sinica.edu.tw.

Journal of Bacteriology, July 2003, p. 4066-4073, Vol. 185, No. 14
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.14.4066-4073.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

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