SHORT COMMUNICATION
Inorganic pyrophosphatase (PPase)
from a higher plant
Publication date: 2014-10-23
BioTechnologia 2013;94(1):35-37
ABSTRACT
Arabidopsis thaliana inorganic pyrophosphatase (AtPPA1) coding DNA (ppa1 gene) was cloned into bacterial expression
vector and overproduced in E. Coli cells as a His-tagged protein. The recombinant protein was purified
from the bacterial lysate by two consecutive chromatographic steps: chelating chromatography on Ni2+-charged
resin followed by FPLC size exclusion chromatography. The homogenous protein was submitted for crystallization.
X-Ray diffraction data extending to 1.9Å resolution were collected using synchrotron radiation. The structure
was solved by molecular replacement and refinement is in progress (R-factor below 20%). The structure of
AtPP1 represents an alpha+beta protein fold which overlaps with other structural models for known bacterial and
yeast inorganic pyrophosphatases.
vector and overproduced in E. Coli cells as a His-tagged protein. The recombinant protein was purified
from the bacterial lysate by two consecutive chromatographic steps: chelating chromatography on Ni2+-charged
resin followed by FPLC size exclusion chromatography. The homogenous protein was submitted for crystallization.
X-Ray diffraction data extending to 1.9Å resolution were collected using synchrotron radiation. The structure
was solved by molecular replacement and refinement is in progress (R-factor below 20%). The structure of
AtPP1 represents an alpha+beta protein fold which overlaps with other structural models for known bacterial and
yeast inorganic pyrophosphatases.
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| eISSN: | 2353-9461 |
| ISSN: | 0860-7796 |
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