A1 Journal article – refereed
Crystal structure of Streptococcus mutans pyrophosphatase: A new fold for an old mechanism




List of 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 number: 9
Issue number: 4
Number of pages: 9
ISSN: 0969-2126

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.

Last updated on 2019-29-01 at 18:31