2MO0

Backbone 1H, 13C, and 15N Chemical Shift Assignments for cold shock protein, TaCsp

2MO0 の概要

• エントリーDOI: 10.2210/pdb2mo0/pdb
• 関連するPDBエントリー: 2MO1
• NMR情報: BMRB: 19915
• 分子名称: Cold-shock DNA-binding domain protein (1 entity in total)
• 機能のキーワード: cold shock protein, thermus aquaticus, protein binding, protein stability, dna binding protein
• 由来する生物種: Thermus aquaticus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7692.65

構造登録者

Jin, B.,Jeong, K.W.,Kim, Y. (登録日: 2014-04-17, 公開日: 2014-08-20, 最終更新日: 2024-05-15)

主引用文献

Jin, B.,Jeong, K.W.,Kim, Y.
Structure and flexibility of the thermophilic cold-shock protein of Thermus aquaticus.
Biochem.Biophys.Res.Commun., 451:402-407, 2014

PubMed Abstract: The thermophilic bacterium Thermus aquaticus is a well-known source of Taq polymerase. Here, we studied the structure and dynamics of the T. aquaticus cold-shock protein (Ta-Csp) to better understand its thermostability using NMR spectroscopy. We found that Ta-Csp has a five-stranded β-barrel structure with five salt bridges which are important for more rigid structure and a higher melting temperature (76 °C) of Ta-Csp compared to mesophilic and psychrophilic Csps. Microsecond to millisecond time scale exchange processes occur only at the β1-β2 surface region of the nucleic acid binding site with an average conformational exchange rate constant of 674 s(-1). The results imply that thermophilic Ta-Csp has a more rigid structure and may not need high structural flexibility to accommodate nucleic acids upon cold shock compared to its mesophile and psychrophile counterparts.

PubMed: 25101648
DOI: 10.1016/j.bbrc.2014.07.127

実験手法

SOLUTION NMR