Structural basis of calcium and galactose recognition by the lectin PA-IL of Pseudomonas aeruginosa
Structural basis of calcium and galactose recognition by the lectin PA-IL of Pseudomonas aeruginosa
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DOI：
10.1016/s0014-5793(03)01249-3
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发表时间：
2003-12-04
期刊：
影响因子：
3.5
通讯作者：
Imberty, A
中科院分区：
文献类型：
--
作者：
Cioci, G;Mitchell, EP;Imberty, A
在1.6埃分辨率下测定与半乳糖和钙复合的四聚体铜绿假单胞菌凝集素I（PA-IL）的结构，并且在2.4埃分辨率下溶解天然蛋白质。每个单体采用在顶点具有配体结合位点的β-夹心折叠。所有的半乳糖羟基，除了O 1，参与与蛋白质的氢键网络和O3和O 4也参与钙离子的配位。钙半乳糖结合的立体化学让人想起在一些动物C型凝集素中观察到的。该复合物的结构为未来设计抗菌化合物提供了框架。(C)2003年欧洲生物化学学会联合会。Elsevier B. V.出版，保留所有权利。
The structure of the tetrameric Pseudomonas aeruginosa lectin I (PA-IL) in complex with galactose and calcium was determined at 1.6 Angstrom resolution, and the native protein was solved at 2.4 Angstrom resolution. Each monomer adopts a beta-sandwich fold with ligand binding site at the apex. All galactose hydroxyl groups, except O1, are involved in a hydrogen bond network with the protein and O3 and O4 also participate in the coordination of the calcium ion. The stereochemistry of calcium galactose binding is reminiscent of that observed in some animal C-type lectins. The structure of the complex provides a framework for future design of anti-bacterial compounds. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.