Modeling and monitoring the effects of three partly conserved Ile residues in the dimerization domain of a Mip-like virulence factor from Escherichia coli
S Seal, T Chakraborty, S Polley, D Paul… - Journal of …, 2024 - Taylor & Francis
FKBP22, an Escherichia coli-made peptidyl-prolyl cis-trans isomerase, has shown
considerable homology with Mip-like virulence factors. While the C-terminal domain of this …
considerable homology with Mip-like virulence factors. While the C-terminal domain of this …
A staphylococcal cyclophilin carries a single domain and unfolds via the formation of an intermediate that preserves cyclosporin A binding activity
S Seal, S Polley, S Sau - Plos one, 2019 - journals.plos.org
Cyclophilin (Cyp), a peptidyl-prolyl cis-trans isomerase (PPIase), acts as a virulence factor in
many bacteria including Staphylococcus aureus. The enzymatic activity of Cyp is inhibited …
many bacteria including Staphylococcus aureus. The enzymatic activity of Cyp is inhibited …
Serine 106 preserves the tertiary structure, function, and stability of a cyclophilin from Staphylococcus aureus
S Seal, N Banerjee, R Mahato, T Kundu… - Journal of …, 2023 - Taylor & Francis
SaCyp, a staphylococcal cyclophilin involved in both protein folding and pathogenesis, has
a Ser residue at position 106 and a Trp residue at position 136. While Ser 106 of SaCyp …
a Ser residue at position 106 and a Trp residue at position 136. While Ser 106 of SaCyp …
Removal of an atypical region from a staphylococcal cyclophilin affects its structure, function, stability, and shape
SaCyp, a cyclophilin having 197 amino acid residues, acts both as a protein-folding catalyst
and a virulence factor in Staphylococcus aureus. Interestingly, a region, homologous to the …
and a virulence factor in Staphylococcus aureus. Interestingly, a region, homologous to the …