ANNUAL REPORT - Department of Biotechnology

Scientist at IISc., Bangalore carried out experiments
for elucidating the significance of glycosylation for
the immunomodulatory activity of glycodelin.
Despite the similarities in overall folding status of
glycodelin and LG, the study revealed that the
stabilizing contacts in the folded conformations of
these proteins are different.
Scientists at CDRI, Lucknow used NMR
spectroscopy to solve structure of Mycobacterium
tuberculosis, Escherichia coli, and Homo sapiens
peptidyl-tRNA hydrolase. The peptidyl-tRNA
hydrolase enzyme is essential for the viability of
bacteria. The ORF Rv1014c of Mycobacterium
tuberculosis H37Rv, labeled as mtpth gene, was
cloned in pET 28b vector and over-expressed in
Escherichia coli BL21 (DE3) cells. A structural
model based on E. coli Pth crystal structure, was
generated.
Oligomerization of PfFabZ
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The malarial parasite Plasmodium falciparum
synthesizes fatty acids by the type II mechanism. In
this cycle, the dehydration of the βhydroxyacyl
acyl carrier protein is
catalyzed by FabZ. Scientists at IISc.,
Bangalore purified FabZ and crystallized using the
hanging-drop vapour-diffusion and microbatch
techniques. The crystal structure PfFabZ has been
determined by molecular replacement method.
PfFabZ has a hot-dog fold and has been found to
exist as a homodimer (d-PfFabZ) in the crystals of the
present study in contrast to the reported hexameric
form (h-PfFabZ) which is a trimer of dimers
crystallized in a different condition. The existence of
the inactive state of the enzyme and the pH triggered
conformational switching between active and
inactive states were revealed by this crystallographic
analysis and provides to new strategies in the design
of novel antimalarials.
Research and Development