Mutational analysis of baculovirus phosphatase identifies structural residues important for triphosphatase activity in vitro and in vivo.
@article{Martins2002MutationalAO, title={Mutational analysis of baculovirus phosphatase identifies structural residues important for triphosphatase activity in vitro and in vivo.}, author={A. Martins and S. Shuman}, journal={Biochemistry}, year={2002}, volume={41 45}, pages={ 13403-9 } }
Baculovirus phosphatase (BVP) and mammalian capping enzyme (Mce1) are members of the RNA triphosphatase branch of the cysteine phosphatase superfamily. Although RNA triphosphatases have a core alpha/beta fold similar to other cysteine phosphatases, there is little conservation of primary structure outside of the cysteine-containing P-loop motif, HCxxxxxR(S/T), that comprises the active site. However, there is extensive primary structure conservation between members of the RNA triphosphatase… CONTINUE READING
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