1T8Y

Crystal Structure of E.coli AMP Nucleosidase complexed with phosphate

Summary for 1T8Y

• Entry DOI: 10.2210/pdb1t8y/pdb
• Related: 1T8R 1T8S 1T8W
• Descriptor: AMP nucleosidase, PHOSPHATE ION (3 entities in total)
• Functional Keywords: alpha-beta-alpha sandwich, alpha-beta fold, hydrolase
• Biological source: Escherichia coli
• Total number of polymer chains: 6
• Total formula weight: 326035.46

Authors

Zhang, Y.,Cottet, S.E.,Ealick, S.E. (deposition date: 2004-05-13, release date: 2004-08-17, Last modification date: 2024-10-16)

Primary citation

Zhang, Y.,Cottet, S.E.,Ealick, S.E.
Structure of Escherichia coli AMP Nucleosidase Reveals Similarity to Nucleoside Phosphorylases
STRUCTURE, 12:1383-1394, 2004

PubMed 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.

PubMed: 15296732
DOI: 10.1016/j.str.2004.05.015

Experimental method

X-RAY DIFFRACTION (3 Å)