The perceived impact of a global pandemic on a provincial department’s organisational structure

Orientation: Several existing studies examine the effect organisational structures have on businesses, but there is limited research that considers the effects unforeseen crises have on organisational structures. Research purpose: The study sought to determine the effects that the coronavirus disease 2019 (COVID-19) pandemic and lockdown had on the organisational structure of a provincial health department, specifically relating to performance management, employee productivity and organisational citizenship behaviour. Motivation for the study: Additional pressure on health workers, who were seen as ‘essential workers’ during the pandemic, motivated the investigation of how organisational structure affects employees’ ability to perform their duties during crises. Research approach/design and method: The study employed a quantitative research approach, using surveys. A non-experimental research method and convenience sampling were employed and a sample of 207 respondents (n = 207) was achieved. Main findings: The respondents agreed that the pandemic did not cause a decline in their performance due to effective workload management. They also agreed that they still felt passionate about their work during the pandemic. They further posited that the pandemic emphasised the importance of teamwork. Practical/managerial implications: The study offers insights into some factors that produced successful outcomes when handling the pandemic, which can inform organisational strategy during any similar future crises. Contribution/value-add: The study adds to the limited literature linking human resources management and change or crisis management, which is critical when navigating a rapidly changing present and an increasingly uncertain workplace future

Oleanolic acid purified from the stem bark of Olax subscorpioidea Oliv. inhibits the function and catalysis of human 17β-hydroxysteroid dehydrogenase 1

Cancer is a leading cause of global death. Medicinal plants have gained increasing attention in cancer drug discovery. In this study, the stem bark extract of Olax subscorpioidea, which is used in ethnomedicine to treat cancer, was subjected to phytochemical investigation leading to the isolation of oleanolic acid (OA). The structure was elucidated by 1-dimensional and 2-dimensional nuclear magnetic resonance spectroscopic (NMR) data, and by comparing its data with previously reported data. Molecular docking was used to investigate the interactions of OA with nine selected cancer-related protein targets. OA docked well with human 17β-hydroxysteroid dehydrogenase type-1 (17βHSD1), caspase-3, and epidermal growth factor receptor tyrosine kinase (binding affinities: –9.8, –9.3, and –9.1 kcal/mol, respectively). OA is a triterpenoid compound with structural similarity to steroids. This similarity with the substrates of 17βHSD1 gives the inhibitor candidate an excellent opportunity to bind to 17βHSD1. The structural and functional dynamics of OA-17βHSD1 were investigated by molecular dynamics simulations at 240 ns. Molecular mechanics/Poisson-Boltzmann surface area (MMPBSA) studies showed that OA had a binding free energy that is comparable with that of vincristine (–52.76, and –63.56 kcal/mol, respectively). The average C-α root mean square of deviation (RMSD) value of OA (1.69 Å) compared with the unbound protein (2.01 Å) indicated its high stability at the protein’s active site. The binding energy and stability at the active site of 17βHSD1 recorded in this study indicate that OA exhibited profound inhibitory potential. OA could be a good scaffold for developing new anti-breast cancer drugs

The intersubunit lock-and-key motif in human glutathione transferase A1-1: role of the key residues Met(51) and Phe(52) in function and dimer stability

The dimeric structure of certain cytosolic GSTs (glutathione S-transferases) is stabilized by a hydrophobic lock-and-key motif at their subunit interface. In hGSTA1-1 (human class Alpha GST with two type-1 subunits), the key consists of two residues, Met(51) and Phe(52), that fit into a hydrophobic cavity (lock) in the adjacent subunit. SEC (size-exclusion chromatography)–HPLC, far-UV CD and tryptophan fluorescence of the M51A and M51A/F52S mutants indicated the non-disruptive nature of these mutations on the global structure. While the M51A mutant retained 80% of wild-type activity, the activity of the M51A/F52S was markedly diminished, indicating the importance of Phe(52) in maintaining the correct conformation at the active site. The M51A and M51A/F52S mutations altered the binding of ANS (8-anilinonaphthalene-l-sulphonic acid) at the H-site by destabilizing helix 9 in the C-terminal region. Data from urea unfolding studies show that the dimer is destabilized by both mutations and that the dimer dissociates to aggregation-prone monomers at low urea concentrations before global unfolding. Although not essential for the assembly of the dimeric structure of hGSTA1-1, both Met(51) and Phe(52) in the intersubunit lock-and-key motif play important structural roles in maintaining the catalytic and ligandin functions and stability of the GST dimer