2RST

NMR structure of the C-terminal domain of EW29

2RST の概要

• エントリーDOI: 10.2210/pdb2rst/pdb
• NMR情報: BMRB: 6226
• 分子名称: 29-kDa galactose-binding lectin (1 entity in total)
• 機能のキーワード: r-type lectin, sugar binding protein
• 由来する生物種: Lumbricus terrestris (Common earthworm)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14877.75

構造登録者

Hemmi, H. (登録日: 2012-05-29, 公開日: 2013-04-17, 最終更新日: 2024-05-15)

主引用文献

Hemmi, H.,Kuno, A.,Hirabayashi, J.
NMR structure and dynamics of the C-terminal domain of R-type lectin from the earthworm Lumbricus terrestris
Febs J., 280:70-82, 2013

PubMed Abstract: The C-terminal domain (Ch; C-half) of the R-type earthworm 29-kDa lectin (EW29), isolated from the earthworm Lumbricus terrestris, has two sugar-binding sites, in subdomains α and γ, and the protein uses the two sugar-binding sites for its function as a single domain-type haemagglutinin. Our previous NMR titration experiments showed that the α sugar-binding site is a high-affinity site and the γ sugar-binding site is a low-affinity site. However, it remains unclear why the α sugar-binding site of EW29Ch binds to lactose much more strongly because the crystal structure of lactose-bound EW29Ch showed that the interaction between the α sugar-binding site and lactose was almost same as that between the γ sugar-binding site and lactose. In the present study, we have determined the NMR structure of EW29Ch in the sugar-free state and performed (15)N relaxation experiments for EW29Ch in both the sugar-free state and the lactose-bound states. The conformation of EW29Ch in the sugar-free state was similar to that of EW29Ch in complex with lactose. Conformational changes upon binding of lactose were observed only for the α sugar-binding site. By contrast, the (15)N relaxation experiments revealed a conformational exchange at the α sugar-binding site in the sugar-free state, which was suppressed in the lactose-bound state. The conformational exchange phenomenon observed for the α sugar-binding site was not observed for the γ sugar-binding site. Differences in the conformational change and the backbone dynamics between subdomains α and γ may be associated with the difference of the sugar-binding modes between the two sugar-binding sites.

PubMed: 23122331
DOI: 10.1111/febs.12050

実験手法

SOLUTION NMR