@article { ISI:000323584400008,
	title = {Structural modelling of substrate binding and inhibition in penicillin V acylase from pectobacterium atrosepticum},
	journal = {Biochemical and Biophysical Research Communications},
	volume = {437},
	number = {4},
	year = {2013},
	month = {AUG},
	pages = {538-543},
	publisher = {ACADEMIC PRESS INC ELSEVIER SCIENCE},
	address = {525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA},
	abstract = {<p>Penicillin V acylases (PVAs) and bile salt hydrolases (BSHs) have considerable sequence and structural similarity; however, they vary significantly in their substrate specificity. We have identified a PVA from a Gram-negative organism, Pectobacterium atrosepticum (PaPVA) that turned out to be a remote homolog of the PVAs and BSHs reported earlier. Even though the active site residues were conserved in PaPVA it showed high specificity towards penV and interestingly the penV acylase activity was inhibited by bile salts. Comparative modelling and docking studies were carried out to understand the structural differences of the binding site that confer this characteristic property. We show that PaPVA exhibits significant differences in structure, which are in contrast to those of known PVAs and such enzymes from Gram-negative bacteria require further investigation. (C) 2013 Elsevier Inc. All rights reserved.</p>},
	keywords = {Bile salt hydrolase, docking, Homology modelling, Inhibition, Pectobacterium, Penicillin acylase},
	issn = {0006-291X},
	doi = {10.1016/j.bbrc.2013.06.109},
	author = {Avinash, Vellore Sunder and Panigrahi, Priyabrata and Suresh, C. G. and Pundle, Archana V. and Ramasamy, Sureshkumar}
}
@article {45643,
	title = {Structural-functional insights and studies on saccharide binding of Sophora japonica seed lectin},
	journal = {International Journal of Biological Macromolecules},
	volume = {91},
	year = {2016},
	month = {OCT},
	pages = {75-84},
	type = {Article},
	abstract = {<p>Functional and conformational transitions of the Sophora japonica seed lectin (SJL) were studied in detail using bioinformatics and biophysical tools. Homology model of the lectin displayed all the characteristics of the legume lectin monomer and the experimental observations correlated well with the structural information. In silico studies were performed by protein-ligand docking, calculating the respective binding energies and the residues involved in the interactions were derived from LigPlot(+) analysis. Fluorescence titrations showed three times higher affinity of T-antigen disaccharide than N-acetyl galactosamine (GaINAc) towards SJL indicating extended sugar binding site of the lectin. Thermodynamic parameters of T-antigen binding to SJL indicated the process to be endothermic and entropically driven while those of GaINAc showed biphasic process. SDS-PAGE showed post-translationally modified homotetrameric species of the lectin under native conditions. In presence of guanidine hydrochloride (0.5-5.0 M), the tetramer first dissociated into dimers followed by unfolding of the protein as indicated by size exclusion chromatography, fluorescence and CD spectroscopy. Different structural rearrangements were observed during thermal denaturation of SJL at physiological pH 7.2, native pH 8.5 and molten globule inducing pH 1.0. Topological information revealed by solute quenching studies at respective pH indicated differential hydrophobic environment and charge density around tryptophan residues. (C) 2016 Elsevier B.V. All rights reserved.</p>},
	keywords = {Dissociation, docking, Homology model, Ligand binding, Sophora japonica seed lectin, Thermal transitions},
	issn = {0141-8130},
	doi = {10.1016/j.ijbiomac.2016.05.047},
	author = {Yadav, Priya and Shahane, Ganesh and Ramasamy, Sureshkumar and Sengupta, Durba and Gaikwad, Sushama}
}
