2DS0
Crystal structure of the earthworm lectin C-terminal domain mutant in complex with 6'-sialyllactose
Summary for 2DS0
| Entry DOI | 10.2210/pdb2ds0/pdb |
| Related | 2AO3 2D12 2DRY 2DRZ |
| Related PRD ID | PRD_900066 |
| Descriptor | 29-kDa galactose-binding lectin, N-acetyl-alpha-neuraminic acid-(2-6)-beta-D-galactopyranose-(1-4)-beta-D-glucopyranose, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | earthworm lumbricus terrestris, sialic acid, galactose, in vitro evolution, beta-trefoil fold, sugar complex, sugar binding protein |
| Biological source | Lumbricus terrestris (common earthworm) |
| Total number of polymer chains | 2 |
| Total formula weight | 30611.73 |
| Authors | Suzuki, R.,Fujimoto, Z. (deposition date: 2006-06-16, release date: 2007-02-06, Last modification date: 2023-10-25) |
| Primary citation | Yabe, R.,Suzuki, R.,Kuno, A.,Fujimoto, Z.,Jigami, Y.,Hirabayashi, J. Tailoring a novel sialic acid-binding lectin from a ricin-B chain-like galactose-binding protein by natural evolution-mimicry J.Biochem., 141:389-399, 2007 Cited by PubMed Abstract: Sialic acid (Sia) is a typical terminal sugar, which modifies various types of glycoconjugates commonly found in higher animals. Its regulatory roles in diverse biological phenomena are frequently triggered by interaction with Sia-binding lectins. When using natural Sia-binding lectins as probes, however, there have been practical problems concerning their repertoire and availability. Here, we show a rational creation of a Sia-binding lectin based on the strategy 'natural evolution-mimicry', where Sia-binding lectins are engineered by error-prone PCR from a Gal-binding lectin used as a scaffold protein. After selection with fetuin-agarose using a recently reinforced ribosome display system, one of the evolved mutants SRC showed substantial affinity for alpha2-6Sia, which the parental Gal-binding lectin EW29Ch lacked. SRC was found to have additional practical advantages in productivity and in preservation of affinity for Gal. Thus, the developed novel Sia-recognition protein will contribute as useful tools to sialoglycomics. PubMed: 17234683DOI: 10.1093/jb/mvm043 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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