The 1.7 Å crystal structure of the C5a peptidase from Streptococcus agalactiae (ScpB) reveals an active site competent for catalysis

被引：1

作者：

Cullen, Ruth ^{[1
]}

Tecza, Malgorzata ^{[1
]}

Miclot, Tom ^{[2
,6
]}

Behan, Senan ^{[1
]}

Jain, Monica ^{[1
]}

Avink, Marjet Klein ^{[3
]}

Cooney, Jakki C. ^{[1
,4
,5
]}

Kagawa, Todd F. ^{[1
,5
]}

机构：

[1] Univ Limerick, Dept Biol Sci, Limerick, Ireland

[2] Lycee Stanislas, Villers De Nancy, France

[3] Univ Appl Sci, Sch Life Sci Engn & Design, Saxion, Netherlands

[4] Univ Limerick, Bernal Inst, Limerick, Ireland

[5] Univ Limerick, SSPC, Limerick, Ireland

[6] Czech Acad Sci, J Heyrovsky Inst Phys Chem, Prague, Czech Republic

来源：

PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS | 2024年 / 92卷 / 03期

基金：

爱尔兰科学基金会;

关键词：

C5a peptidase; ScpA; ScpB; specificity; streptococcal virulence; GROUP-A; SUITE;

D O I：

10.1002/prot.26625

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A 1.7 angstrom 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 (similar to 20 angstrom) 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 RMSDC alpha (4.6 angstrom). The fold of the active form of ScpB is nearly identical to ScpA (RMSDC alpha 0.2 angstrom), 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.

引用

页码：427 / 431

页数：5

共 24 条

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