The results of the structural studies of bacterial oligopeptidase B (OpB) belonging to the least well-studied prolyl oligopeptidase family are described. The screening of crystallization conditions for mutants of the enzyme, its complexes with peptides, which mimic substrates and catalytic reaction products, and a complex with a transition state analog as an inhibitor was performed in order to determine the three-dimensional structures of OpB from Serratia proteamaculans (PSP) acting at different steps of the catalytic cycle. Crystals suitable for X-ray diffraction were grown. The X-ray diffraction data sets were collected, processed, and subjected to preliminary analysis. These X-ray diffraction data sets are suitable for obtaining the structural data necessary for the description of the catalytic cycle of bacterial OpBs.
Petrenko DE, Nikolaeva AY, Lazarenko VA, Dorovatovskiy PV, Timofeev VI, Vlaskina AV, Korzhenevskiy DA, Mikhailova AG, Boyko KM, Rakitina TV (2020) Crystallographic Study of Mutants and Complexes of Oligopeptidase B from Serratia proteamaculans Crystallogr Rep65: 909-914
Petrenko DE, Nikolaeva AY, Lazarenko VA, Dorovatovskiy PV, Timofeev VI, Vlaskina AV, Korzhenevskiy DA, Mikhailova AG, Boyko KM, Rakitina TV (2020) Crystallogr Rep65: 909-914