Summary for 2ZQN
Entry DOI | 10.2210/pdb2zqn/pdb |
Related | 2DRY 2DRZ 2DS0 2ZQO |
Related PRD ID | PRD_900004 |
Descriptor | 29-kDa galactose-binding lectin, beta-D-galactopyranose-(1-4)-beta-D-glucopyranose, PHOSPHATE ION, ... (5 entities in total) |
Functional Keywords | earthworm lumbricus terrestris, hemagglutinin, r-type lectin, beta-trefoil fold, sugar complex, lectin, sugar binding protein |
Biological source | Lumbricus terrestris (Common earthworm) |
Total number of polymer chains | 2 |
Total formula weight | 31190.40 |
Authors | Suzuki, R.,Kuno, A.,Hasegawa, T.,Hirabayashi, J.,Kasai, K.,Momma, M.,Fujimoto, Z. (deposition date: 2008-08-13, release date: 2008-09-02, Last modification date: 2023-11-01) |
Primary citation | Suzuki, R.,Kuno, A.,Hasegawa, T.,Hirabayashi, J.,Kasai, K.,Momma, M.,Fujimoto, Z. Sugar-complex structures of the C-half domain of the galactose-binding lectin EW29 from the earthworm Lumbricus terrestris Acta Crystallogr.,Sect.D, 65:49-57, 2009 Cited by PubMed Abstract: R-type lectins are one of the most prominent types of lectin; they exist ubiquitously in nature and mainly bind to the galactose unit of sugar chains. The galactose-binding lectin EW29 from the earthworm Lumbricus terrestris belongs to the R-type lectin family as represented by the plant lectin ricin. It shows haemagglutination activity and is composed of a single peptide chain that includes two homologous domains: N-terminal and C-terminal domains. A truncated mutant of EW29 comprising the C-terminal domain (rC-half) has haemagglutination activity by itself. In order to clarify how rC-half recognizes ligands and shows haemagglutination activity, X-ray crystal structures of rC-half in complex with D-lactose and N-acetyl-D-galactosamine have been determined. The structure of rC-half is similar to that of the ricin B chain and consists of a beta-trefoil fold; the fold is further divided into three similar subdomains referred to as subdomains alpha, beta and gamma, which are gathered around the pseudo-threefold axis. The structures of sugar complexes demonstrated that subdomains alpha and gamma of rC-half bind terminal galactosyl and N-acetylgalactosaminyl glycans. The sugar-binding properties are common to both ligands in both subdomains and are quite similar to those of ricin B chain-lactose complexes. These results indicate that the C-terminal domain of EW29 uses these two galactose-binding sites for its function as a single-domain-type haemagglutinin. PubMed: 19153466DOI: 10.1107/S0907444908037451 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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