Structural Aspects for the Recognition of ATP by Ribonucleopeptide Receptors

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• 作者：Shun Nakano ; Tsukasa Mashima ; Akimasa Matsugami ; Masafumi Inoue ; Masato Katahira ; Takashi Morii
• 刊名：Journal of the American Chemical Society
• 出版年：2011
• 出版时间：March 30, 2011
• 年：2011
• 卷：133
• 期：12
• 页码：4567-4579
• 全文大小：1226K
• 年卷期：v.133,no.12(March 30, 2011)
• ISSN：1520-5126

文摘

A modular structure of ribonucleopeptide (RNP) affords a framework to construct macromolecular receptors and fluorescent sensors. We have isolated ATP-binding RNP with the minimum of nucleotides for ATP binding, in which the RNA consensus sequence is different from those reported for RNA aptamers against the ATP analogues. The three-dimensional structure of the substrate-binding complex of RNP was studied to understand the ATP-binding mechanism of RNP. A combination of NMR measurements, enzymatic and chemical mapping, and nucleotide mutation studies of the RNP-adenosine complex show that RNP interacts with the adenine ring of adenosine by forming a U:A:U triple with two invariant U nucleotides. The observed recognition mode for the adenine ring is different from those of RNA aptamers for ATP derivatives reported previously. The RNP-adenosine complex is folded into a particular structure by formation of the U:A:U triple and a Hoogsteen type A:U base pair. This recognition mechanism was successfully utilized to convert the substrate-binding specificity of RNP from ATP- to GTP-binding with a C⁺:G:C triple recognition mode.