TdfH selectively binds metal-loaded tetrameric calprotectin for zinc import.
Commun Biol
; 5(1): 103, 2022 01 31.
Article
in En
| MEDLINE
| ID: mdl-35102276
ABSTRACT
To combat nutritional immunity, N. gonorrhoeae has evolved systems to hijack zinc and other metals directly from host metal-binding proteins such as calprotectin (CP). Here, we report the 6.1 Å cryoEM structure of the gonococcal surface receptor TdfH in complex with a zinc-bound CP tetramer. We further show that TdfH can also interact with CP in the presence of copper and manganese, but not with cobalt.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Bacterial Outer Membrane Proteins
/
Zinc
/
Leukocyte L1 Antigen Complex
/
Neisseria gonorrhoeae
Type of study:
Prognostic_studies
Language:
En
Journal:
Commun Biol
Year:
2022
Document type:
Article
Affiliation country:
United States