Structural highlights
1t8r is a 6 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| NonStd Res: | |
| Related: | 1t8s, 1t8w, 1t8y |
| Gene: | AMN, B1982, Z3139, ECS2779 ("Bacillus coli" Migula 1895) |
| Activity: | AMP nucleosidase, with EC number 3.2.2.4 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[AMN_ECOLI] Involved in regulation of AMP concentrations.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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:http://dx.doi.org/10.1016/j.str.2004.05.015
