2ITH

NMR Structure of Haloferax volcanii DHFR

2ITH の概要

• エントリーDOI: 10.2210/pdb2ith/pdb
• NMR情報: BMRB: 6645
• 分子名称: Dihydrofolate reductase (1 entity in total)
• 機能のキーワード: oxidoreductase, dihydrofolate reductase, dhfr, halophilic archaea
• 由来する生物種: Haloferax volcanii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17983.79

構造登録者

Binbuga, B. (登録日: 2006-10-19, 公開日: 2007-09-04, 最終更新日: 2024-05-01)

主引用文献

Binbuga, B.,Boroujerdi, A.F.,Young, J.K.
Structure in an extreme environment: NMR at high salt.
Protein Sci., 16:1783-1787, 2007

PubMed Abstract: Proteins from halophiles have adapted to challenging environmental conditions and require salt for their structure and function. How halophilic proteins adapted to a hypersaline environment is still an intriguing question. It is important to mimic the physiological conditions of the archae extreme halophiles when characterizing their enzymes, including structural characterization. The NMR derived structure of Haloferax volcanii dihydrofolate reductase in 3.5 M NaCl is presented, and represents the first high salt structure calculated using NMR data. Structure calculations show that this protein has a solution structure which is similar to the previously determined crystal structure with a difference at the N terminus of beta3 and the type of beta-turn connection beta7 and beta8.

PubMed: 17656587
DOI: 10.1110/ps.072950407

実験手法

SOLUTION NMR