A CONSERVED SECONDARY STRUCTURAL MOTIF IN 23S RIBOSOMAL-RNA DEFINES THE SITE OF INTERACTION OF AMICETIN, A UNIVERSAL INHIBITOR OF PEPTIDE-BOND FORMATION
A CONSERVED SECONDARY STRUCTURAL MOTIF IN 23S RIBOSOMAL-RNA DEFINES THE SITE OF INTERACTION OF AMICETIN, A UNIVERSAL INHIBITOR OF PEPTIDE-BOND FORMATION
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DOI：
10.1002/j.1460-2075.1994.tb06432.x
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发表时间：
1994-04-01
期刊：
影响因子：
11.4
通讯作者：
MANKIN, AS
中科院分区：
文献类型：
--
作者：
LEVIEV, IG;RODRIGUEZFONSECA, C;MANKIN, AS
抑制肽键形成的通用抗生素阿米西丁的结合位点和可能的作用位点已经确定。来自体内突变体、定点突变和化学足迹的证据都表明，靠近结构域 V 中心环的 23S 样 rRNA 二级结构中存在高度保守的飞蛾。我们推断该基序位于或接近肽基转移中心的催化位点。阿米西丁的结合位点是一组功能相关的己糖-胞嘧啶抑制剂中第一个位于核糖体上的结合位点。
The binding site and probable site of action have been determined for the universal antibiotic amicetin which inhibits peptide bond formation. Evidence from in vivo mutants, site-directed mutations and chemical footprinting all implicate a highly conserved moth in the secondary structure of the 23S-like rRNA close to the central circle of domain V. We infer that this motif lies at, or close to, the catalytic site in the peptidyl transfer centre. The binding site of amicetin is the first of a group of functionally related hexose-cytosine inhibitors to be localized on the ribosome.