2JOI

NMR solution structure of hypothetical protein TA0095 from Thermoplasma acidophilum

2JOI の概要

• エントリーDOI: 10.2210/pdb2joi/pdb
• 分子名称: Hypothetical protein Ta0095 (1 entity in total)
• 機能のキーワード: protein, structural genomics, thermoplasma acidophilum, cog4004 orthologous group, structural genomics consortium, sgc, unknown function
• 由来する生物種: Thermoplasma acidophilum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13596.45

構造登録者

Jimenez, M.,Leon, E.,Santoro, J.,Rico, M.,Yee, A.,Structural Genomics Consortium (SGC) (登録日: 2007-03-13, 公開日: 2007-10-02, 最終更新日: 2023-12-20)

主引用文献

Leon, E.,Yee, A.,Ortiz, A.R.,Santoro, J.,Rico, M.,Jimenez, M.A.
Solution structure of the hypothetical protein TA0095 from Thermoplasma acidophilum: A novel superfamily with a two-layer sandwich architecture
Protein Sci., 16:2278-2286, 2007

PubMed Abstract: TA0095 is a 96-residue hypothetical protein from Thermoplasma acidophilum that exhibits no sequence similarity to any protein of known structure. Also, TA0095 is a member of the COG4004 orthologous group of unknown function found in Archaea bacteria. We determined its three-dimensional structure by NMR methods. The structure displays an alpha/beta two-layer sandwich architecture formed by three alpha-helices and five beta-strands following the order beta1-alpha1-beta2-beta3-beta4-beta5-alpha2-alpha3. Searches for structural homologs indicate that the TA0095 structure belongs to the TBP-like fold, constituting a novel superfamily characterized by an additional C-terminal helix. The TA0095 structure provides a fold common to the COG4004 proteins that will obviously belong to this new superfamily. Most hydrophobic residues conserved in the COG4004 proteins are buried in the structure determined herein, thus underlying their importance for structure stability. Considering that the TA0095 surface shows a large positively charged patch with a high degree of residue conservation within the COG4004 domain, the biological function of TA0095 and the rest of COG4004 proteins might occur through binding a negatively charged molecule. Like other TBP-like fold proteins, the COG4004 proteins might be DNA-binding proteins. The fact that TA0095 is shown to interact with large DNA fragments is in favor of this hypothesis, although nonspecific DNA binding cannot be ruled out.

PubMed: 17766377
DOI: 10.1110/ps.072869607

実験手法

SOLUTION NMR