1t8s

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{{STRUCTURE_1t8s| PDB=1t8s | SCENE= }}
{{STRUCTURE_1t8s| PDB=1t8s | SCENE= }}
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'''Crystal Structure of E.coli AMP Nucleosidase complexed with formicin 5'-monophosphate'''
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===Crystal Structure of E.coli AMP Nucleosidase complexed with formicin 5'-monophosphate===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15296732 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15296732}}
==About this Structure==
==About this Structure==
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[[Category: Alpha-beta fold]]
[[Category: Alpha-beta fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:40:48 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:23:40 2008''

Revision as of 16:23, 28 July 2008

Image:1t8s.png

Template:STRUCTURE 1t8s

Crystal Structure of E.coli AMP Nucleosidase complexed with formicin 5'-monophosphate

Template:ABSTRACT PUBMED 15296732

About this Structure

1T8S is a Single protein structure of sequence from Escherichia coli. 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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