8GO7

Fungal immunomodulatory protein FIP-nha N5+39A

8GO7 の概要

• エントリーDOI: 10.2210/pdb8go7/pdb
• 分子名称: Fungal immunomodulatory protein FIP-nha (2 entities in total)
• 機能のキーワード: immunomodulatory, anti-tumor, thermostable, hydrolysis resistance, immune system
• 由来する生物種: Fusarium haematococcum
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 56022.10

構造登録者

Liu, Y.,Bastiaan-Net, S.,Hoppenbrouwers, T.,Li, Z.,Wichers, H.J. (登録日: 2022-08-24, 公開日: 2023-08-30, 最終更新日: 2023-09-20)

主引用文献

Liu, Y.,Hoppenbrouwers, T.,Wang, Y.,Xie, Y.,Wei, X.,Zhang, H.,Du, G.,Imam, K.M.S.U.,Wichers, H.,Li, Z.,Bastiaan-Net, S.
Glycosylation Contributes to Thermostability and Proteolytic Resistance of rFIP-nha ( Nectria haematococca ).
Molecules, 28:-, 2023

PubMed Abstract: Glycosylation is an important post-translational modification of proteins, contributing to protein function, stability and subcellular localization. Fungal immunomodulatory proteins (FIPs) are a group of small proteins with notable immunomodulatory activity, some of which are glycoproteins. In this study, the impact of glycosylation on the bioactivity and biochemical characteristics of FIP-nha (from ) is described. Three rFIP-nha glycan mutants (N5A, N39A, N5+39A) were constructed and expressed in to study the functionality of the specific N-glycosylation on amino acid N5 and N39. Their protein characteristics, structure, stability and activity were tested. WT and mutants all formed tetramers, with no obvious difference in crystal structures. Their melting temperatures were 82.2 °C (WT), 81.4 °C (N5A), 80.7 °C (N39A) and 80.1 °C (N5+39A), indicating that glycosylation improves thermostability of rFIP-nha. Digestion assays showed that glycosylation on either site improved pepsin resistance, while 39N-glycosylation was important for trypsin resistance. Based on the 3D structure and analysis of enzyme cleavage sites, we conclude that glycosylation might interfere with hydrolysis via increasing steric hindrance. WT and mutants exerted similar bioactivity on tumor cell metabolism and red blood cells hemagglutination. Taken together, these findings indicate that glycosylation of FIP-nha impacts its thermostability and digestion resistance.

PubMed: 37687215
DOI: 10.3390/molecules28176386

実験手法

X-RAY DIFFRACTION (2.303 Å)