2RST
NMR structure of the C-terminal domain of EW29
Summary for 2RST
| Entry DOI | 10.2210/pdb2rst/pdb |
| NMR Information | BMRB: 6226 |
| Descriptor | 29-kDa galactose-binding lectin (1 entity in total) |
| Functional Keywords | r-type lectin, sugar binding protein |
| Biological source | Lumbricus terrestris (Common earthworm) |
| Total number of polymer chains | 1 |
| Total formula weight | 14877.75 |
| Authors | Hemmi, H. (deposition date: 2012-05-29, release date: 2013-04-17, Last modification date: 2024-05-15) |
| Primary citation | 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 Cited by 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: 23122331DOI: 10.1111/febs.12050 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
