2MF6

Solution NMR structure of Chimeric Avidin, ChiAVD(I117Y), in the biotin bound form

2MF6 の概要

• エントリーDOI: 10.2210/pdb2mf6/pdb
• 関連するPDBエントリー: 3MM0
• NMR情報: BMRB: 18125
• 分子名称: Avidin, Avidin-related protein 4/5 (1 entity in total)
• 機能のキーワード: biotin binding protein
• 由来する生物種: Gallus gallus (chicken)
• 細胞内の位置: Secreted: P02701
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 57601.02

構造登録者

Tossavainen, H.,Kukkurainen, S.,Maatta, J.A.E.,Pihlajamaa, T.,Hytonen, V.P.,Kulomaa, M.S.,Permi, P. (登録日: 2013-10-07, 公開日: 2014-08-06, 最終更新日: 2024-11-06)

主引用文献

Tossavainen, H.,Kukkurainen, S.,Maatta, J.A.E.,Kahkonen, N.,Pihlajamaa, T.,Hytonen, V.P.,Kulomaa, M.S.,Permi, P.
Chimeric Avidin - NMR Structure and Dynamics of a 56 kDa Homotetrameric Thermostable Protein
Plos One, 9:e100564-e100564, 2014

PubMed Abstract: Chimeric avidin (ChiAVD) is a product of rational protein engineering remarkably resistant to heat and harsh conditions. In quest of the fundamentals behind factors affecting stability we have elucidated the solution NMR spectroscopic structure of the biotin-bound form of ChiAVD and characterized the protein dynamics through 15N relaxation and hydrogen/deuterium (H/D) exchange of this and the biotin-free form. To surmount the challenges arising from the very large size of the protein for NMR spectroscopy, we took advantage of its high thermostability. Conventional triple resonance experiments for fully protonated proteins combined with methyl-detection optimized experiments acquired at 58°C were adequate for the structure determination of this 56 kDa protein. The model-free parameters derived from the 15N relaxation data reveal a remarkably rigid protein at 58°C in both the biotin-bound and the free forms. The H/D exchange experiments indicate a notable increase in hydrogen protection upon biotin binding.

PubMed: 24959850
DOI: 10.1371/journal.pone.0100564

実験手法

SOLUTION NMR