A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä
Crystal structure of Streptococcus mutans pyrophosphatase: A new fold for an old mechanism
Tekijät: Merckel MC, Fabrichniy IP, Salminen A, Kalkkinen N, Baykov AA, Lahti R, Goldman A
Kustantaja: CELL PRESS
Julkaisuvuosi: 2001
Journal: Structure
Tietokannassa oleva lehden nimi: STRUCTURE
Lehden akronyymi: STRUCTURE
Vuosikerta: 9
Numero: 4
Aloitussivu: 289
Lopetussivu: 297
Sivujen määrä: 9
ISSN: 0969-2126
DOI: https://doi.org/10.1016/S0969-2126(01)00587-1
Tiivistelmä
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.
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.
Turun yliopiston Tutkimustietojärjestelmän portaali