PMID:15296732
| Citation |
Zhang, Y, Cottet, SE and Ealick, SE (2004) Structure of Escherichia coli AMP nucleosidase reveals similarity to nucleoside phosphorylases. Structure 12:1383-94 |
|---|---|
| Abstract |
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 A resolution, and structures of the complexes with either formycin 5'-monophosphate or inorganic phosphate were determined at 2.6 A and 3.0 A 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. |
| Links |
PubMed Online version:10.1016/j.str.2004.05.015 |
| Keywords |
Amino Acid Sequence; Catalytic Domain; Crystallography, X-Ray; Escherichia coli/enzymology; Formycins/chemistry; Models, Molecular; Molecular Sequence Data; N-Glycosyl Hydrolases/chemistry; Pentosyltransferases/chemistry; Phosphates/chemistry; Ribonucleotides/chemistry; Ribosemonophosphates/chemistry; Sequence Homology, Amino Acid |
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