Structural and biochemical characterization of the Clostridium perfringens-specific Zn
Amidase
Bacterial cell wall
Clostridium perfringens
Endolysin
Peptidoglycan
Journal
Biochemical and biophysical research communications
ISSN: 1090-2104
Titre abrégé: Biochem Biophys Res Commun
Pays: United States
ID NLM: 0372516
Informations de publication
Date de publication:
22 10 2021
22 10 2021
Historique:
received:
06
08
2021
accepted:
27
08
2021
pubmed:
6
9
2021
medline:
22
12
2021
entrez:
5
9
2021
Statut:
ppublish
Résumé
Phage-derived endolysins, enzymes that degrade peptidoglycans, have the potential to serve as alternative antimicrobial agents. Psa, which was identified as an endolysin encoded in the genome of Clostridium perfringens st13, was shown to specifically lyse C. perfringens. Psa has an N-terminal catalytic domain that is homologous to the Amidase_2 domain (PF01510), and a novel C-terminal cell wall-binding domain. Here, we determined the X-ray structure of the Psa catalytic domain (Psa-CD) at 1.65 Å resolution. Psa-CD has a typical Amidase_2 domain structure, consisting of a spherical structure with a central β-sheet surrounded by two α-helix groups. Furthermore, there is a Zn
Identifiants
pubmed: 34482025
pii: S0006-291X(21)01267-5
doi: 10.1016/j.bbrc.2021.08.085
pii:
doi:
Substances chimiques
Peptidoglycan
0
Endopeptidases
EC 3.4.-
endolysin
EC 3.4.99.-
Amidohydrolases
EC 3.5.-
amidase
EC 3.5.1.4
Zinc
J41CSQ7QDS
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
66-72Informations de copyright
Copyright © 2021 Elsevier Inc. All rights reserved.