High-Resolution Single-Particle Cryo-EM Hydrated Structure of
Journal
Biochemistry
ISSN: 1520-4995
Titre abrégé: Biochemistry
Pays: United States
ID NLM: 0370623
Informations de publication
Date de publication:
07 02 2023
07 02 2023
Historique:
pubmed:
27
1
2023
medline:
9
2
2023
entrez:
26
1
2023
Statut:
ppublish
Résumé
Cellular plasminogen (Pg) receptors (PgRs) are utilized to recruit Pg; stimulate its activation to the serine protease, plasmin (Pm); and sterically protect the surface Pm from inactivation by host inhibitors. One such PgR is the moonlighting enzyme, enolase, some of which leaves the cytoplasm and resides at the cell surface to potentially function as a PgR. Since microbes employ conscription of host Pg by PgRs as one virulence mechanism, we explored the structural basis of the ability of
Identifiants
pubmed: 36701429
doi: 10.1021/acs.biochem.2c00637
doi:
Substances chimiques
Plasminogen
9001-91-6
Bacterial Proteins
0
Phosphopyruvate Hydratase
EC 4.2.1.11
Lysine
K3Z4F929H6
Carrier Proteins
0
Serine Proteases
EC 3.4.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM