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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

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posted on 2023-11-13, 15:51 authored by Ruth Cullen, Malgorzata Teçza, Tom Miclot, Senan Behan, Monica Jain, Marjet Klein Avink, JAKKI COONEYJAKKI COONEY, Todd KagawaTodd Kagawa

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 (4.6 Å). The fold of the active form of ScpB is nearly identical to ScpA (RMSD 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.

Funding

SSPC_Phase 2

Science Foundation Ireland

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History

Publication

Proteins. 2023, pp. 1-5

Publisher

Wiley and Sons Ltd

Other Funding information

Monica Jain and Ruth Cullen were in receipt of Irish Research Council Government of Ireland Postgraduate Scholarships. Malgorzata Teçza was funded through the Government of Ireland Disruptive Technologies Fund (grant DT20180054). Todd F. Kagawa was funded through Science Foundation Ireland (grants 21/FFP-P/10109 12/RC/2275_P2 to Jakki C. Cooney). This work was supported by Enterprise Ireland Commercialisation Fund CF/2013/3336 to Jakki C. Cooney. Open access funding provided by IReL.

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  • Bernal Institute

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  • Biological Sciences

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