Structural basis of glmS ribozyme activation by glucosamine-6-phosphate
Structural basis of glmS ribozyme activation by glucosamine-6-phosphate
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DOI：
10.1126/science.1129666
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发表时间：
2006-09-22
期刊：
影响因子：
56.9
通讯作者：
Ferre-D'Amare, Adrian R.
中科院分区：
文献类型：
--
作者：
Klein, Daniel J.;Ferre-D'Amare, Adrian R.
GLMS核酶是已知的唯一需要小分子活化剂才能催化的天然催化RNA。这种催化的RNA发挥核糖开关的作用，依赖于激活剂的RNA裂解调节GLMS信使RNA的表达。我们报道了GLMS核酶在未连接或结合竞争抑制剂葡萄糖-6-磷酸的裂解前状态和裂解后状态的晶体结构。所有的结构都紧密地重叠在一起，揭示了一个非常刚性的RNA，它包含一个预先形成的活性和辅酶结合位点。与其他核糖开关不同，GLMS核酶将其激活剂结合在一个开放的、溶剂可及的口袋中。我们的结构表明，GLMS核酶结合的辅酶的氨基执行一般的酸碱和静电催化。
The glmS ribozyme is the only natural catalytic RNA known to require a small-molecule activator for catalysis. This catalytic RNA functions as a riboswitch, with activator-dependent RNA cleavage regulating glmS messenger RNA expression. We report crystal structures of the glmS ribozyme in precleavage states that are unliganded or bound to the competitive inhibitor glucose-6-phosphate and in the postcleavage state. All structures superimpose closely, revealing a remarkably rigid RNA that contains a preformed active and coenzyme-binding site. Unlike other riboswitches, the glmS ribozyme binds its activator in an open, solvent-accessible pocket. Our structures suggest that the amine group of the glmS ribozyme-bound coenzyme performs general acid-base and electrostatic catalysis.