Abstract
A 1.7 Å structure is presented for an active form of the virulence factor ScpB, the C5a peptidase from Streptococcus agalactiae. The previously reported structure of the ScpB active site mutant exhibited a large separation (~20 Å) between the catalytic His and Ser residues. Significant differences are observed in the catalytic domain between the current and mutant ScpB structures resulting with a high RMSDCα (4.6 Å). The fold of the active form of ScpB is nearly identical to ScpA (RMSDCα 0.2 Å), the C5a-peptidase from Streptococcus pyogenes. Both ScpA and ScpB have comparable activity against human C5a, indicating neither enzyme require host proteins for C5a-ase activity. These studies are a first step in resolving reported differences in the specificities of these enzymes.
Original language | English |
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Pages (from-to) | 427-431 |
Number of pages | 5 |
Journal | Proteins: Structure, Function and Genetics |
Volume | 92 |
Issue number | 3 |
DOIs | |
Publication status | Published - Mar 2024 |
Keywords
- C5a peptidase
- ScpA
- ScpB
- specificity
- streptococcal virulence