3MM0

Crystal structure of chimeric avidin

3MM0 の概要

• エントリーDOI: 10.2210/pdb3mm0/pdb
• 関連するPDBエントリー: 1Y53 2AVI
• 分子名称: Avidin, Avidin-related protein 4/5 (2 entities in total)
• 機能のキーワード: avidin, avr4, high affinity systems, hyper-thermostability, biotin binding protein
• 由来する生物種: Gallus gallus (bantam,chickens); 詳細
• 細胞内の位置: Secreted: P02701
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 172803.05

構造登録者

Livnah, O.,Eisenberg-Domovich, Y.,Maatta, J.A.E.,Kulomaa, M.S.,Hytonen, V.P.,Nordlund, H.R. (登録日: 2010-04-19, 公開日: 2010-10-27, 最終更新日: 2024-10-16)

主引用文献

Maatta, J.A.,Eisenberg-Domovich, Y.,Nordlund, H.R.,Hayouka, R.,Kulomaa, M.S.,Livnah, O.,Hytonen, V.P.
Chimeric avidin shows stability against harsh chemical conditions-biochemical analysis and 3D structure.
Biotechnol.Bioeng., 108:481-490, 2011

PubMed Abstract: Avidin and its bacterial analog streptavidin have been widely used in applications in life sciences. Recently, we described a highly thermostable engineered avidin, called chimeric avidin, which is a hybrid of avidin and avidin-related protein 4. Here, we report a protocol for pilot-scale production in E. coli and the X-ray structure of chimeric avidin. The ligand-binding properties of chimeric avidin were explored with isothermal titration calorimetry. We found chimeric avidin to be more stable against various harsh organic solvents at elevated temperatures compared to avidin and streptavidin. The properties of chimeric avidin make it a potential tool for new applications in biotechnology.

PubMed: 20939005
DOI: 10.1002/bit.22962

実験手法

X-RAY DIFFRACTION (2.7 Å)