Structure of ristocetin A in complex with a bacterial cell-wall mimetic.
Structure of ristocetin A in complex with a bacterial cell-wall mimetic.
复制标题
瑞斯托菌素 A 与细菌细胞壁模拟物复合物的结构。
DOI：
10.1107/s0907444909018344
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发表时间：
2009
期刊：
影响因子：
--
通讯作者：
Loll,PatrickJ
中科院分区：
文献类型：
--
作者：
Nahoum,Virginie;Spector,Sherri;Loll,PatrickJ
Antimicrobial drug resistance is a serious public health problem and the development of new antibiotics has become an important priority. Ristocetin A is a class III glycopeptide antibiotic that is used in the diagnosis of von Willebrand disease and which has served as a lead compound for the development of new antimicrobial therapeutics. The 1.0 Å resolution crystal structure of the complex between ristocetin A and a bacterial cell-wall peptide has been determined. As is observed for most other glycopeptide antibiotics, it is shown that ristocetin A forms a back-to-back dimer containing concave binding pockets that recognize the cell-wall peptide. A comparison of the structure of ristocetin A with those of class I glycopeptide antibiotics such as vancomycin and balhimycin identifies differences in the details of dimerization and ligand binding. The structure of the ligand-binding site reveals a likely explanation for ristocetin A's unique anticooperativity between dimerization and ligand binding.
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