1JYS

Crystal Structure of E. coli MTA/AdoHcy Nucleosidase

Summary for 1JYS

• Entry DOI: 10.2210/pdb1jys/pdb
• Descriptor: MTA/SAH nucleosidase, ADENINE (3 entities in total)
• Functional Keywords: mixed alpha/beta, dimer, hydrolase
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 51246.50

Authors

Lee, J.E.,Cornell, K.A.,Riscoe, M.K.,Howell, P.L. (deposition date: 2001-09-13, release date: 2002-10-01, Last modification date: 2024-02-07)

Primary citation

Lee, J.E.,Cornell, K.A.,Riscoe, M.K.,Howell, P.L.
Structure of E. coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase reveals similarity to the purine nucleoside phosphorylases.
Structure, 9:941-953, 2001

PubMed Abstract: 5'-methylthioadenosine/S-adenosyl-homocysteine (MTA/AdoHcy) nucleosidase catalyzes the irreversible cleavage of 5'-methylthioadenosine and S-adenosylhomocysteine to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. While this enzyme is crucial for the metabolism of AdoHcy and MTA nucleosides in many prokaryotic and lower eukaryotic organisms, it is absent in mammalian cells. This metabolic difference represents an exploitable target for rational drug design.

PubMed: 11591349
DOI: 10.1016/S0969-2126(01)00656-6

Experimental method

X-RAY DIFFRACTION (1.9 Å)