1UDV

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

1UDV の概要

• エントリーDOI: 10.2210/pdb1udv/pdb
• 分子名称: DNA binding protein SSO10b, ZINC ION (3 entities in total)
• 機能のキーワード: dna binding protein
• 由来する生物種: Sulfolobus solfataricus
• 細胞内の位置: Cytoplasm (Probable): Q97ZF4
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 20577.17

構造登録者

Chou, C.-C.,Lin, T.-W.,Chen, C.-Y.,Wang, A.H.J. (登録日: 2003-05-07, 公開日: 2003-08-05, 最終更新日: 2023-12-27)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.85 Å)