2IX9

Respective role of protein folding and glycosylation in the thermal stability of recombinant Feruloyl Esterase A

2IX9 の概要

• エントリーDOI: 10.2210/pdb2ix9/pdb
• 関連するPDBエントリー: 1USW 1UWC 1UZA 2BJH
• 分子名称: FERULOYL ESTERASE A, 3-CYCLOHEXYL-1-PROPYLSULFONIC ACID, 1,2-ETHANEDIOL, ... (5 entities in total)
• 機能のキーワード: hydrolase, xylan degradation, feruloyl esterase ec 3.1.1.73, glycoprotein, serine esterase
• 由来する生物種: ASPERGILLUS NIGER
• 細胞内の位置: Secreted: O42807
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 57877.14

構造登録者

Sulzenbacher, G.,Benoit, I. (登録日: 2006-07-07, 公開日: 2006-10-18, 最終更新日: 2024-10-23)

主引用文献

Benoit, I.,Asther, M.,Sulzenbacher, G.,Record, E.,Marmuse, L.,Parsiegla, G.,Gimbert, I.,Asther, M.,Bignon, C.
Respective Importance of Protein Folding and Glycosylation in the Thermal Stability of Recombinant Feruloyl Esterase A.
FEBS Lett., 580:5815-, 2006

PubMed Abstract: The thermal stability of four molecular forms (native, refolded, glycosylated, non-glycosylated) of feruloyl esterase A (FAEA) was studied. From the most to the least thermo-resistant, the four molecular species ranked as follows: (i) glycosylated form produced native, (ii) non-glycosylated form produced native, (iii) non-glycosylated form produced as inclusion bodies and refolded, and (iv) glycosylated form produced native chemically denatured and then refolded. On the basis of these results and of crystal structure data, we discuss the respective importance of protein folding and glycosylation in the thermal stability of recombinant FAEA.

PubMed: 17027758
DOI: 10.1016/J.FEBSLET.2006.09.039

実験手法

X-RAY DIFFRACTION (1.7 Å)