Comparative Analysis of the Active Sites of Orthologous Endolysins of the Escherichia Lytic Bacteriophages T5, RB43, and RB49
Document Type
Article
Publication Date
2021
Digital Object Identifier (DOI)
https://doi.org/10.1016/j.ijbiomac.2020.10.264
Abstract
The methods of solution NMR, circular dichroism (CD), and differential scanning calorimetry (DSC) were used to study two zinc-containing L-alanyl-D-glutamate peptidases - endolysins of the pseudo T-even myoviruses RB43 and RB49 (EndoRB43 and EndoRB49, respectively), which are orthologous to the EndoT5, which is a zinc-containing L-alanyl-D-glutamate peptidase of the T5 siphovirus. The spatial conservation of the Zn2+-binding sites for the enzymes EndoT5, EndoRB43, and EndoRB49 was established, and the key role of Zn2+ ions in the stabilization of the spatial structures of these three peptidases was confirmed. We are showing here that the binding of the Zn2+ ion in the active center of EndoRB49 peptidase causes conformational rearrangements similar to those observed in the EndoT5 peptidase upon binding of Zn2+ and Ca2+ ions and lead to the formation of a catalytically active form of the enzyme. Therefore, the binding of the Zn2+ ion to the active site of EndoRB49 peptidase is a necessary and sufficient condition for functioning of this protein.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
International Journal of Biological Macromolecules, v. 166, p. 1096-1105
Scholar Commons Citation
Kutyshenko, Victor P.; Prokhorov, Dmitry A.; Mikoulinskaia, Galina V.; Molochkov, Nikolai V.; Yegorov, Alexander Y.; Paskevich, Svetlana I.; and Uversky, Vladimir N., "Comparative Analysis of the Active Sites of Orthologous Endolysins of the Escherichia Lytic Bacteriophages T5, RB43, and RB49" (2021). Molecular Medicine Faculty Publications. 206.
https://digitalcommons.usf.edu/mme_facpub/206
