1IX5

Solution structure of the Methanococcus thermolithotrophicus FKBP

1IX5 の概要

• エントリーDOI: 10.2210/pdb1ix5/pdb
• NMR情報: BMRB: 4668
• 分子名称: FKBP (1 entity in total)
• 機能のキーワード: fkbp fold, ppiase, isomerase
• 由来する生物種: Methanothermococcus thermolithotrophicus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16825.96

構造登録者

Suzuki, R.,Nagata, K.,Kawakami, M.,Nemoto, N.,Furutani, M.,Adachi, K.,Maruyama, T.,Tanokura, M. (登録日: 2002-06-12, 公開日: 2003-06-10, 最終更新日: 2023-12-27)

主引用文献

Suzuki, R.,Nagata, K.,Yumoto, F.,Kawakami, M.,Nemoto, N.,Furutani, M.,Adachi, K.,Maruyama, T.,Tanokura, M.
Three-dimensional Solution Structure of an Archaeal FKBP with a Dual Function of Peptidyl Prolyl cis-trans Isomerase and Chaperone-like Activities
J.MOL.BIOL., 328:1149-1160, 2003

PubMed Abstract: Here we report the solution structure of an archaeal FK506-binding protein (FKBP) from a thermophilic archaeum, Methanococcus thermolithotrophicus (MtFKBP17), which has peptidyl prolyl cis-trans isomerase (PPIase) and chaperone-like activities, to reveal the structural basis for the dual function. In addition to a typical PPIase domain, a newly identified domain is formed in the flap loop by a 48-residue insert that is required for the chaperone-like activity. The new domain, called IF domain (the Insert in the Flap), is a novel-folding motif and exposes a hydrophobic surface, which we consider to play an important role in the chaperone-like activity.

PubMed: 12729748
DOI: 10.1016/S0022-2836(03)00379-6

実験手法

SOLUTION NMR