1fyu | pdb_00001fyu

Crystal structure of erythrina corallodendron lectin in hexagonal crystal form

spinqualitylabelsall models 1fyu, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1fyu is a 2 chain structure with sequence from Erythrina corallodendron. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, GLC, MN, GAL Related: 1axy, 1axz, 1ax0, 1ax1, 1ax2, 1lte Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [LEC_ERYCO] Galactose and N-acetyllactosamine specific lectin. Binds to the H-2 blood type determinant fucosyl-N-acetyllactosamine. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The Erythrina corallodendron lectin (EcorL) crystallizes in monoclinic and hexagonal crystal forms. Comparison of the newly determined hexagonal form (PDB code 1fyu) with the monoclinic form shows that the dimeric structure of EcorL reflects the inherent biological structure of the protein and is not an artifact of the crystal packing. To further understand the factors determining the dimerization modes of legume lectins, EcorL, concanavalin A (ConA), and Griffonia simplicifolia (GS4) were taken as representatives of the three unique dimers found in the family. Six virtual homodimers were generated. The hydropathy, amino acid composition, and solvation energy were calculated for all nine homodimers. Each of the three native dimers has a distinct chemical composition. EcorL has a dominant hydrophobic component, and ConA has a strong polar component, but in GS4 the three components contribute equally to the interface. This distribution pattern at the interface is unique to the native dimers and distinct from the partition observed in the virtual dimers. Amino acid composition of other members of the family that dimerize like EcorL or ConA maintain the same pattern of amino acids distribution observed in EcorL and ConA. However, lectins that dimerize like GS4 do not show a particularly distinct distribution. In all cases, the calculated solvation energy of the native dimer was lower than that of the virtual dimers, suggesting that the observed mode of dimerization is the most stable organization for the given sequence and tertiary structure. The dimerization type cannot be predicted by sequence analysis. Chemical characteristics of dimer interfaces in the legume lectin family.,Elgavish S, Shaanan B Protein Sci. 2001 Apr;10(4):753-61. PMID:11274466 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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