2A2Y

NMR Structue of Sso10b2 from Sulfolobus solfataricus

2A2Y の概要

• エントリーDOI: 10.2210/pdb2a2y/pdb
• NMR情報: BMRB: 5892
• 分子名称: DNA/RNA-binding protein Alba 2 (1 entity in total)
• 機能のキーワード: hyperthermophile protein, dimer, dna, rna 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: 20511.76

構造登録者

Biyani, K.,Kahsai, M.A.,Clark, A.T.,Armstrong, T.L.,Edmondson, S.P.,Shriver, J.W. (登録日: 2005-06-23, 公開日: 2005-11-08, 最終更新日: 2024-05-22)

主引用文献

Biyani, K.,Kahsai, M.A.,Clark, A.T.,Armstrong, T.L.,Edmondson, S.P.,Shriver, J.W.
Solution structure, stability, and nucleic Acid binding of the hyperthermophile protein sso10b2.
Biochemistry, 44:14217-14230, 2005

PubMed Abstract: The Sso10b (or Alba) family of proteins is a conserved group of archaeal and eukaryotic proteins which are thought to play a role in both chromatin organization and RNA metabolism. We describe here the solution structure and properties of Sso10b2 from Sulfolobus solfataricus. NMR data including residual dipolar couplings and (15)N relaxation data demonstrated that the protein adopts a beta(1)alpha(1)beta(2)alpha(2)beta(3)beta(4) topology with an IF-3-like fold. The protein dimerizes in solution at 30 degrees C via a hydrophobic surface defined by the C-terminal alpha(2)beta(3)beta(4) elements with a structure similar to one of the putative dimers indicated by previous crystal structures. DSC and circular dichroism data demonstrated an unusual two-state structural transition near the growth temperature which led to an increase in beta-sheet content without dissociation of the dimer. The cooperativity of the transition exceeded that of a dimer at pH 7, demonstrating the presence of higher order oligomers near the growth temperature at pH 7. Reverse titrations of Sso10b2 with nucleic acid showed that the protein binds single-stranded DNA (K(d) of 3 x 10(-)(7) M) with higher affinity than RNA (1.3 x 10(-)(6) M) or double-stranded DNA (1.5 x 10(-)(5) M) in 10 mM KH(2)PO(4) (pH 7.0, 20 degrees C). NMR chemical shift perturbation data indicated that single-stranded DNA and RNA binding occurred across the same dimer interface and encompassed a surface defined by the C-terminal ends of the beta(1), beta(2), and beta(3) strands of each monomer.

PubMed: 16245938
DOI: 10.1021/bi051266r

実験手法

SOLUTION NMR