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Related Experiment Video

Updated: Aug 18, 2025

Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD

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Published on: December 30, 2016

X-ray diffraction data for the C5a-peptidase mutant with modified activity and specificity.

Todd F Kagawa^1,2, Monica Jain¹, Jakki C Cooney^1,3,2

¹Department of Biological Sciences, University of Limerick, Limerick, Ireland.

|December 8, 2022

Summary

Streptococcal C5a peptidase (ScpA) inactivates human complement factor C5a. A D783A mutation in ScpA significantly reduced substrate binding, and its crystal structure was determined to understand this specificity.

Keywords:

C5a peptidase Enzyme activity Exosite Immunomodulatory enzymes Mutant Substrate binding

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Last Updated: Aug 18, 2025

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Analysis of SEC-SAXS data via EFA deconvolution and Scatter

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Published on: January 28, 2021

Area of Science:

Biochemistry
Structural Biology
Complement System

Background:

Streptococcal C5a peptidase (ScpA) inactivates human complement factor C5a (hC5a), a target for COVID-19 treatment.
Understanding ScpA's substrate selectivity is crucial for therapeutic engineering.
hC5a binding involves electrostatic interactions with ScpA's Fn2 domain exosite.

Purpose of the Study:

To elucidate the structural basis for ScpA's specificity.
To analyze the impact of a D783A mutation on ScpA's structure and function.
To present the X-ray crystal structure of the ScpA D783A mutant.

Main Methods:

X-ray crystallography (1.9 Å resolution) of the ScpA D783A mutant.
Molecular replacement for structure solution.
Surface plasmon resonance (SPR) and enzyme kinetics (previously reported).

Main Results:

The 1.9 Å X-ray diffraction data for ScpA D783A were obtained.
The molecular replacement solution for the ScpA D783A structure was determined.
The D783A mutation significantly reduces substrate binding affinity and catalytic activity (kcat).

Conclusions:

The crystal structure of ScpA D783A provides insights into the role of the Fn2 exosite in substrate recognition.
Structural data complements SPR and kinetic analyses, explaining the reduced activity and affinity.
This work aids in engineering ScpA for therapeutic applications targeting the complement system.