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Note:
Structural Biology 2018 & STD AIDS 2018
Journal of Genetics and Molecular Biology
|
Volume 2
S e p t e m b e r 0 3 - 0 4 , 2 0 1 8 | B a n g k o k , T h a i l a n d
allied
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STD-AIDS AND INFECTIOUS DISEASES
STRUCTURAL BIOLOGY AND PROTEOMICS
&
International Conference on
International Conference on
Joint Event on
Umesh Yadava, J Genet Mol Biol 2018, Volume 2
SOLUTE BINDING PROTEINS AND THEIR
COGNATE LIGANDS: STRUCTURE,
FUNCTION AND THEIR ROLE IN
FUNCTIONAL ANNOTATION
Umesh Yadava
Deen Dayal Upadhyaya Gorakhpur University, India
T
he uptake of exogenous solutes is mediated by transport systems
embedded in the plasma membrane and drive active transport even at
µM to nM solute concentrations. In many of these systems a periplasmic
Solute-Binding Protein (SBP) is utilized to bind their cognate ligands with
high affinity and deliver them to the membrane bound translocator subunits.
Active transport systems with SBP components are traditionally divided into
three main families based on their energetic coupling mechanism, primary
sequence and subunit composition: tripartite ATP-independent periplasmic
transporters (TRAP), ATP binding cassette transporters (ABC) and tripartite
tricarboxylate transporters (TTT). Knowledge of the cognate ligand for the
SBP component of the transporter can provide crucial data for functional
assignment of co-located or co-regulated genes. In the present study, the
structural and functional characterizations of several solute binding proteins
have been carried out. Proteins were cloned from genomic DNA, expressed
by autoinduction and purified by a combination of Ni-NTA and size exclusion
chromatography. The purified SBPs were screened using differential
scanning fluorometry (DSF) and a >400 compounds ligand library. Two of the
SBPs exhibited DSF hits that were novel for their respective transport family.
Crystallization trials of proteins have been conducted with their respective
DSF ligand hits. Those SBPs that have structures determined and their
respective interactions with co-crystallized ligands will be presented. Co-
crystallization with DSF determined ligands resulted in structures of Avi_5305
in complex with D-glucosamine and D-galactosamine, the first structure of an
ABC SBP with an amino sugar.
Umesh Yadava has started his career as Lecturer at
MGPG College, Gorakhpur in 2001. He joined Depart-
ment of Physics, DDU Gorakhpur University in 2003.
He is the recipient of DST Young Scientist under FAST
Track Scheme, and UGC Raman Fellowship awards.
He has one-year postdoctoral research experience at
AECOM, New York, USA.
u_yadava@yahoo.comBIOGRAPHY