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BioTechnologia
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1/2013
vol. 94
 
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abstract:
Short communication

Inorganic pyrophosphatase (PPase) from a higher plant

Marta Grzechowiak
,
Michał Sikorski
,
Mariusz Jaskolski

BioTechnologia vol. 94(1) C pp. 35-37 C 2013
Online publish date: 2014/10/23
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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.


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