Structure of Escherichia coli AMP nucleosidase reveals similarity to nucleoside phosphorylases.
Structure of Escherichia coli AMP nucleosidase reveals similarity to nucleoside phosphorylases.
复制标题
大肠杆菌 AMP 核苷酶的结构与核苷磷酸化酶相似。
DOI：
10.1016/j.str.2004.05.015
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发表时间：
2004
期刊：
影响因子：
--
通讯作者：
Ealick,StevenE
中科院分区：
文献类型：
--
作者：
Zhang,Yang;Cottet,SarahE;Ealick,StevenE
AMP nucleosidase (AMN) catalyzes the hydrolysis of AMP to form adenine and ribose 5-phosphate. The enzyme is found only in prokaryotes, where it plays a role in purine nucleoside salvage and intracellular AMP level regulation. Enzyme activity is stimulated by ATP and suppressed by phosphate. The structure of unliganded AMN was determined at 2.7 Å resolution, and structures of the complexes with either formycin 5′-monophosphate or inorganic phosphate were determined at 2.6 Å and 3.0 Å resolution, respectively. AMN is a biological homohexamer, and each monomer is composed of two domains: a catalytic domain and a putative regulatory domain. The overall topology of the catalytic domain and some features of the substrate binding site resemble those of the nucleoside phosphorylases, demonstrating that AMN is a new member of the family. The structure of the regulatory domain consists of a long helix and a four-stranded sheet and has a novel topology.
