1gzc

High-Resolution crystal structure of Erythrina cristagalli lectin in complex with lactose

spinqualitylabelsall models 1gzc, resolution 1.58Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1gzc is a 1 chain structure with sequence from Erythrina crista-galli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.58Å Ligands: BGC, CA, GAL, MN, PRD_900004 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function LEC_ERYCG 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 primary sequence of Erythrina cristagalli lectin (ECL) was mapped by mass spectrometry, and the crystal structures of the lectin in complex with lactose and 2'-alpha-L-fucosyllactose were determined at 1.6A and 1.7A resolution, respectively. The two complexes were compared with the crystal structure of the closely related Erythrina corallodendron lectin (ECorL) in complex with lactose, with the crystal structure of the Ulex europaeus lectin II in complex with 2'-alpha-L-fucosyllactose, and with two modeled complexes of ECorL with 2'-alpha-L-fucosyl-N-acetyllactosamine. The molecular models are very similar to the crystal structure of ECL in complex with 2'-alpha-L-fucosyllactose with respect to the overall mode of binding, with the L-fucose fitting snugly into the cavity surrounded by Tyr106, Tyr108, Trp135 and Pro134 adjoining the primary combining site of the lectin. Marked differences were however noted between the models and the experimental structure in the network of hydrogen bonds and hydrophobic interactions holding the L-fucose in the combining site of the lectin, pointing to limitations of the modeling approach. In addition to the structural characterization of the ECL complexes, an effort was undertaken to correlate the structural data with thermodynamic data obtained from microcalorimetry, revealing the importance of the water network in the lectin combining site for carbohydrate binding. High-resolution crystal structures of Erythrina cristagalli lectin in complex with lactose and 2'-alpha-L-fucosyllactose and correlation with thermodynamic binding data.,Svensson C, Teneberg S, Nilsson CL, Kjellberg A, Schwarz FP, Sharon N, Krengel U J Mol Biol. 2002 Aug 2;321(1):69-83. PMID:12139934 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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