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|1t8r, resolution 2.70Å ()|
|Gene:||AMN, B1982, Z3139, ECS2779 (Escherichia coli)|
|Related:||1t8s, 1t8w, 1t8y|
Crystal Structure of E. coli AMP Nucleosidase
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.
Structure of Escherichia coli AMP nucleosidase reveals similarity to nucleoside phosphorylases., Zhang Y, Cottet SE, Ealick SE, Structure. 2004 Aug;12(8):1383-94. PMID:15296732
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
- Zhang Y, Cottet SE, Ealick SE. Structure of Escherichia coli AMP nucleosidase reveals similarity to nucleoside phosphorylases. Structure. 2004 Aug;12(8):1383-94. PMID:15296732 doi:10.1016/j.str.2004.05.015
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