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The 1.7 Å crystal structure of the C5a peptidase from Streptococcus agalactiae (ScpB) reveals an active site competent for catalysis.
- Source :
-
Proteins [Proteins] 2024 Mar; Vol. 92 (3), pp. 427-431. Date of Electronic Publication: 2023 Nov 03. - Publication Year :
- 2024
-
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 RMSD <subscript>Cα</subscript> (4.6 Å). The fold of the active form of ScpB is nearly identical to ScpA (RMSD <subscript>Cα</subscript> 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.<br /> (© 2023 The Authors. Proteins: Structure, Function, and Bioinformatics published by Wiley Periodicals LLC.)
Details
- Language :
- English
- ISSN :
- 1097-0134
- Volume :
- 92
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Proteins
- Publication Type :
- Academic Journal
- Accession number :
- 37921533
- Full Text :
- https://doi.org/10.1002/prot.26625