Cryo-EM reveals unique structural features of the FhuCDB Escherichia coli ferrichrome importer.
Journal
Communications biology
ISSN: 2399-3642
Titre abrégé: Commun Biol
Pays: England
ID NLM: 101719179
Informations de publication
Date de publication:
09 12 2021
09 12 2021
Historique:
received:
23
07
2021
accepted:
24
11
2021
entrez:
10
12
2021
pubmed:
11
12
2021
medline:
11
1
2022
Statut:
epublish
Résumé
As one of the most elegant biological processes developed in bacteria, the siderophore-mediated iron uptake demands the action of specific ATP-binding cassette (ABC) importers. Although extensive studies have been done on various ABC importers, the molecular basis of these iron-chelated-siderophore importers are still not fully understood. Here, we report the structure of a ferrichrome importer FhuCDB from Escherichia coli at 3.4 Å resolution determined by cryo electron microscopy. The structure revealed a monomeric membrane subunit of FhuB with a substrate translocation pathway in the middle. In the pathway, there were unique arrangements of residues, especially layers of methionines. Important residues found in the structure were interrogated by mutagenesis and functional studies. Surprisingly, the importer's ATPase activity was decreased upon FhuD binding, which deviated from the current understanding about bacterial ABC importers. In summary, to the best of our knowledge, these studies not only reveal a new structural twist in the type II ABC importer subfamily, but also provide biological insights in the transport of iron-chelated siderophores.
Identifiants
pubmed: 34887516
doi: 10.1038/s42003-021-02916-2
pii: 10.1038/s42003-021-02916-2
pmc: PMC8660799
doi:
Substances chimiques
ATP-Binding Cassette Transporters
0
Escherichia coli Proteins
0
FhuC protein, E coli
0
Membrane Transport Proteins
0
Periplasmic Binding Proteins
0
Siderophores
0
fhuB protein, E coli
105634-64-8
fhuD protein, E coli
112002-32-1
Ferrichrome
15630-64-5
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
1383Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM126626
Pays : United States
Organisme : NIA NIH HHS
ID : R21 AG064572
Pays : United States
Organisme : NIGMS NIH HHS
ID : U24 GM129547
Pays : United States
Commentaires et corrections
Type : ErratumIn
Informations de copyright
© 2021. The Author(s).
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