Copper Forms a PPII Helix-Like Structure with the Catalytic Domains of Bacterial Zinc Metalloproteases.
Journal
Inorganic chemistry
ISSN: 1520-510X
Titre abrégé: Inorg Chem
Pays: United States
ID NLM: 0366543
Informations de publication
Date de publication:
13 Nov 2023
13 Nov 2023
Historique:
medline:
14
11
2023
pubmed:
1
11
2023
entrez:
1
11
2023
Statut:
ppublish
Résumé
The rapid spread of antibiotic-resistant bacteria continuously raises concerns about the future ineffectiveness of current antimicrobial treatments against infectious diseases. To address this problem, new therapeutic strategies and antimicrobial drugs with unique modes of action are urgently needed. Inhibition of metalloproteases, bacterial virulence factors, is a promising target for the development of antibacterial treatments. In this study, the interaction among Zn(II), Cu(II), and the metal-binding domains of two metalloproteases, AprA (
Identifiants
pubmed: 37909295
doi: 10.1021/acs.inorgchem.3c02391
pmc: PMC10647932
doi:
Substances chimiques
Copper
789U1901C5
Zinc
J41CSQ7QDS
polyproline
25191-13-3
Peptides
0
Coordination Complexes
0
Amino Acids
0
Amines
0
Metalloproteases
EC 3.4.-
Anti-Infective Agents
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
18425-18439Références
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