CH鈭捪€ 鈥淭-Shape鈥?Interaction with Histidine Explains Binding of Aromatic Galactosides to Pseudomonas aeruginosa Lectin LecA
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- 作者：Rameshwar U. Kadam ; Divita Garg ; Julian Schwartz ; Ricardo Visini ; Michael Sattler ; Achim Stocker ; Tamis Darbre ; Jean-Louis Reymond
- 刊名：ACS Chemical Biology
- 出版年：2013
- 出版时间：September 20, 2013
- 年：2013
- 卷：8
- 期：9
- 页码：1925-1930
- 全文大小：368K
- 年卷期：v.8,no.9(September 20, 2013)
- ISSN：1554-8937
文摘
The galactose specific lectin LecA mediates biofilm formation in the opportunistic pathogen P. aeruginosa. The interaction between LecA and aromatic 尾-galactoside biofilm inhibitors involves an intermolecular CH鈭捪€ T-shape interaction between C(蔚1)鈥揌 of residue His50 in LecA and the aromatic ring of the galactoside aglycone. The generality of this interaction was tested in a diverse family of 尾-galactosides. LecA binding to aromatic 尾-galactosides (KD 8 渭M) was consistently stronger than to aliphatic 尾-galactosides (KD 36 渭M). The CH鈭捪€ interaction was observed in the X-ray crystal structures of six different LecA complexes, with shorter than the van der Waals distances indicating productive binding. Related XH/cation/蟺鈥撓€ interactions involving other residues were identified in complexes of aromatic glycosides with a variety of carbohydrate binding proteins such as concanavalin A. Exploiting such interactions might be generally useful in drug design against these targets.