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Structural basis of the substrate specificity of Bacillus cereus adenosine phosphorylase by Paola Dessanti; Yang Zhang; Simone Allegrini; Maria Grazia Tozzi; Francesco Sgarrella; Steven E. Ealick is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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Purine nucleoside phosphorylases catalyze the phosphorolytic cleavage of the glycosidic bond of purine (2 0 -deoxy)nucleosides, generating the corresponding free base and (2 0 -deoxy)ribose 1-phosphate. Two classes of PNPs have been identified: homotrimers specific for 6-oxopurines and homohexamers that accept both 6-oxopurines and 6-aminopurines. Bacillus cereus adenosine phosphorylase (AdoP) is a hexameric PNP; however, it is highly specific for 6-aminopurines. To investigate the structural basis for the unique substrate specificity of AdoP, the active-site mutant D204N was prepared and kinetically characterized and the structures of the wild-type protein and the D204N mutant complexed with adenosine and sulfate or with inosine and sulfate were determined at high resolution (1.2-1.4 A ̊). AdoP interacts directly with the preferred substrate through a hydrogen-bond donation from the catalytically important residue Asp204 to N7 of the purine base. Comparison with Escherichia coli PNP revealed a more optimal orientation of Asp204 towards N7 of adenosine and a more closed active site. When inosine is bound, two water molecules are interposed between Asp204 and the N7 and O6 atoms of

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Author

Paola Dessanti; Yang Zhang; Simone Allegrini; Maria Grazia Tozzi; Francesco Sgarrella; Steven E. Ealick

Publisher

International Union of Crystallography; Blackwell Publishing Inc.; International Union of Crystallography (IUCr) (ISSN 0907-4449)

Published

2012

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)