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adenylate kinase (Adk):
In all organisms adenylate kinases (Adks) play a vital
role in cellular energy metabolism and nucleic acid synthesis.
Due to differences in catalytic properties between the Adks
found in prokaryotes and in the cytoplasm of eukaryotes, there
is interest in targeting this enzyme for new drug therapies
against infectious bacterial agents. We present here the
three-dimensional protein structure of Burkholderia
pseudomallei Adk. This pathogen is an aerobic,
Gram-negative, soil-dwelling bacterium responsible for the
infectious disease melioidosis, which is a serious health
problem in Northern Australia and Southeast Asia and accounts
for 40% of all sepsis-related mortality in northeast Thailand.
Due to its potential use in biological warfare and biological
terrorism, B. pseudomallei is also of concern to the U.S.
Centers for Disease Control and Prevention. An unexpected
feature of the BpAdk crystal structure was the observation of
two significantly different conformations of the protein in the
same protein crystal. In the figure, the two molecules (purple
and blue) are superpositioned. The regions in green are the
corresponding highly conserved hinge regions. We propose that
the different conformations represent two snapshots of BpAdk as
it progresses towards a closed, enzymatically active state. The
two conformations of BpAdk observed in the crystal structure
reported here represent two more structure snapshots to further
study the relationships between enzyme structure, dynamics, and
function.
For more information, please see the Protein Data Bank entry
3gmt. This work is published in Biochem Bioph Res Comm
(2010) 394:1012–1017.

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