Crystal structure of Streptococcus mutans pyrophosphatase: A new fold for an old mechanism

: Merckel MC, Fabrichniy IP, Salminen A, Kalkkinen N, Baykov AA, Lahti R, Goldman A

Publisher: CELL PRESS

: 2001

: Structure

: STRUCTURE

: 9

: 4

: 289

: 297

: 9

: 0969-2126

DOI: https://doi.org/10.1016/S0969-2126(01)00587-1

Conclusions: The active site similiarities, including a water coordinated to two metal ions, suggest that the family II PPase mechanism is "analogous" (not "homologous") to that of family I PPases. This is a remarkable example of convergent evolution. The large change in C-terminal conformation suggests that domain closure might be the mechanism by which Sm-PPase achieves specificity for pyrophosphate over other polyphosphates.

Biochemistry, cell and molecular biology