A1 Refereed original research article in a scientific journal
Crystal structure of Streptococcus mutans pyrophosphatase: A new fold for an old mechanism
Authors: Merckel MC, Fabrichniy IP, Salminen A, Kalkkinen N, Baykov AA, Lahti R, Goldman A
Publisher: CELL PRESS
Publication year: 2001
Journal: Structure
Journal name in source: STRUCTURE
Journal acronym: STRUCTURE
Volume: 9
Issue: 4
First page : 289
Last page: 297
Number of pages: 9
ISSN: 0969-2126
DOI: https://doi.org/10.1016/S0969-2126(01)00587-1
Abstract
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.
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