1GZC

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

1GZC の概要

• エントリーDOI: 10.2210/pdb1gzc/pdb
• 関連するPDBエントリー: 1GZ9
• 関連するBIRD辞書のPRD_ID: PRD_900004
• 分子名称: ERYTHRINA CRISTA-GALLI LECTIN, beta-D-galactopyranose-(1-4)-beta-D-glucopyranose, MANGANESE (II) ION, ... (5 entities in total)
• 機能のキーワード: lectin, carbohydrate, sugar binding protein, saccharide, protein-carbohydrate interactions, lactose, glycoprotein
• 由来する生物種: ERYTHRINA CRISTA-GALLI (COCKSPUR CORAL TREE)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26686.50

構造登録者

Svensson, C.,Krengel, U. (登録日: 2002-05-17, 公開日: 2002-06-21, 最終更新日: 2023-12-13)

主引用文献

Svensson, C.,Teneberg, S.,Nilsson, C.,Kjellberg, A.,Schwarz, F.,Sharon, N.,Krengel, U.
High-Resolution Crystal Structures of Erythrina Cristagalli Lectin in Complex with Lactose and 2'-Alpha-L-Fucosyllactose and Correlation with Thermodynamic Binding Data
J.Mol.Biol., 321:69-, 2002

PubMed Abstract: 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.

PubMed: 12139934
DOI: 10.1016/S0022-2836(02)00554-5

実験手法

X-RAY DIFFRACTION (1.58 Å)