2M1H

Solution structure of a PWWP domain from Trypanosoma brucei

2M1H の概要

• エントリーDOI: 10.2210/pdb2m1h/pdb
• NMR情報: BMRB: 18474
• 分子名称: Transcription elongation factor S-II (1 entity in total)
• 機能のキーワード: transcription factor, transcription
• 由来する生物種: Trypanosoma brucei
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13247.49

構造登録者

Wang, R.,Fan, K.,Liao, S.,Zhang, J.,Tu, X. (登録日: 2012-11-28, 公開日: 2013-12-04, 最終更新日: 2024-05-15)

主引用文献

Wang, R.,Zhang, J.,Liao, S.,Tu, X.
Solution structure of TbTFIIS2-1 PWWP domain from Trypanosoma brucei.
Proteins, 84:912-919, 2016

PubMed Abstract: TbTFIIS2-1, one of the two TFIIS homologues of Trypanosome brucei (T. brucei), cooperates with TbTFIIS1 in regulating transcription in T. brcuei. Structurally divergent from other TFIIS homologues from higher organisms, TbTFIIS2-1 contains an additional N-terminal PWWP domain besides other three conserved domains, which may imply potential role of TbTFIIS2-1 in transcription regulation. Here, we determined the solution structure of PWWP domain of TbTFIIS2-1 by NMR spectroscopy, which was the first solution structure of PWWP domain solved in trypanosomatid. In spite of poor sequence similarity between PWWP domains, this domain of TbTFIIS2-1 adopts a conserved 3D-structure, which contains a five-stranded β-barrel and a C-terminal α-helix. Furthermore, we found that TbTFIIS2-1 PWWP domain may be a protein-protein interaction module without the ability of DNA recognition and methyl-group interaction. Proteins 2016; 84:912-919. © 2016 Wiley Periodicals, Inc.

PubMed: 27005948
DOI: 10.1002/prot.25035

実験手法

SOLUTION NMR