1t8y
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(New page: 200px<br /><applet load="1t8y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t8y, resolution 3.00Å" /> '''Crystal Structure of...)
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Revision as of 00:57, 21 November 2007
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Crystal Structure of E.coli AMP Nucleosidase complexed with phosphate
Overview
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.
About this Structure
1T8Y is a Single protein structure of sequence from Escherichia coli with PO4 as ligand. Active as AMP nucleosidase, with EC number 3.2.2.4 Full crystallographic information is available from OCA.
Reference
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
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