Structural basis of the substrate specificity of Bacillus cereus adenosine phosphorylase

Adenosine phosphorylase from B. cereus shows a strong preference for adenosine over other 6-oxopurine nucleosides. Mutation of Asp204 to asparagine reduces the efficiency of adenosine cleavage but does not affect inosine cleavage, effectively reversing the substrate specificity. The structures of D204N complexes explain these observations.

A corrected space group for Sulfolobus sulfataricus 5'-deoxy-5'-methylthioadenosine phosphorylase II

The structure of 5'-deoxy-5'-methylthioadenosine phosphorylase II was incorrectly reported in space group P1 with pseudo-R32 symmetry. Post-analysis showed that the correct space group is C2, a maximal non-isomorphic subgroup of space group R32.