Structural features of the Cu²⁺–vancomycin complex

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• 作者：Marzena Kucharczyk ; Magdalena Brzezowska ; Anna Macią ; g ; Tadeusz Lis ; Mał ; gorzata Jeż ; owska-Bojczuk
• 关键词：Glycopeptide antibiotics ; Vancomycin ; Copper coordination ; Crystal structure
• 刊名：Journal of Inorganic Biochemistry
• 出版年：2008
• 出版时间：April 2008
• 年：2008
• 卷：102
• 期：4
• 页码：936-942
• 全文大小：678 K

文摘

The structure of vancomycin coordinated to Cu²⁺ ions is presented and structural aspects upon metal coordination are discussed. The asymmetric part of unit cell comprises two independent molecules of vancomycin–Cu²⁺ complex, one of them is partially disordered. The binding site involves one imino nitrogen atom, two amide nitrogen atoms delivered by peptide bonds, and carboxyl oxygen from the peptide moiety. The identical set of donor atoms is not reflected in identical coordination geometry around individual metal ions. The studied complex presents two distinct types of conformation. Additionally, leucinyl side chain in one conformer is disordered leading to another type of conformation. The complex molecules form heterodimer with antiparallel hydrogen bonding.