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Page 41

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

academies

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.com

BIOGRAPHY