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2ZQN

Crystal structure of the earthworm R-type lectin C-half in complex with Lactose

Replaces:  2D12
Summary for 2ZQN
Entry DOI10.2210/pdb2zqn/pdb
Related2DRY 2DRZ 2DS0 2ZQO
Related PRD IDPRD_900004
Descriptor29-kDa galactose-binding lectin, beta-D-galactopyranose-(1-4)-beta-D-glucopyranose, PHOSPHATE ION, ... (5 entities in total)
Functional Keywordsearthworm lumbricus terrestris, hemagglutinin, r-type lectin, beta-trefoil fold, sugar complex, lectin, sugar binding protein
Biological sourceLumbricus terrestris (Common earthworm)
Total number of polymer chains2
Total formula weight31190.40
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 citationSuzuki, 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: 19153466
DOI: 10.1107/S0907444908037451
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

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