1UDV

Crystal structure of the hyperthermophilic archaeal dna-binding protein Sso10b2 at 1.85 A

Summary for 1UDV

• Entry DOI: 10.2210/pdb1udv/pdb
• Descriptor: DNA binding protein SSO10b, ZINC ION (3 entities in total)
• Functional Keywords: dna binding protein
• Biological source: Sulfolobus solfataricus
• Cellular location: Cytoplasm (Probable): Q97ZF4
• Total number of polymer chains: 2
• Total formula weight: 20577.17

Authors

Chou, C.-C.,Lin, T.-W.,Chen, C.-Y.,Wang, A.H.J. (deposition date: 2003-05-07, release date: 2003-08-05, Last modification date: 2023-12-27)

Primary citation

Chou, C.C.,Lin, T.W.,Chen, C.Y.,Wang, A.H.J.
Crystal structure of the hyperthermophilic archaeal DNA-binding protein Sso10b2 at a resolution of 1.85 Angstroms
J.BACTERIOL., 185:4066-4073, 2003

PubMed 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.

PubMed: 12837780
DOI: 10.1128/JB.185.14.4066-4073.2003

Experimental method

X-RAY DIFFRACTION (1.85 Å)