8BTY

Structure of the active form of ScpB, the C5a-peptidase from Streptococcus agalactiae.

8BTY の概要

• エントリーDOI: 10.2210/pdb8bty/pdb
• 分子名称: C5a peptidase, MALONIC ACID, SULFATE ION, ... (7 entities in total)
• 機能のキーワード: c5a-peptidase, virulence factor, hydrolase
• 由来する生物種: Streptococcus agalactiae
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 221187.66

構造登録者

Kagawa, T.F.,Cooney, J.C.,Miclot, T.,Cullen, R. (登録日: 2022-11-30, 公開日: 2023-11-15, 最終更新日: 2024-02-14)

主引用文献

Cullen, R.,Tecza, M.,Miclot, T.,Behan, S.,Jain, M.,Avink, M.K.,Cooney, J.C.,Kagawa, T.F.
The 1.7 angstrom crystal structure of the C5a peptidase from Streptococcus agalactiae (ScpB) reveals an active site competent for catalysis.
Proteins, 92:427-431, 2024

PubMed 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 (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.

PubMed: 37921533
DOI: 10.1002/prot.26625

実験手法

X-RAY DIFFRACTION (1.7 Å)