Structural Features Mediating Zinc Binding and Transfer in the AztABCD Zinc Transporter System.
ABC transporter
chaperone
metal homeostasis
zinc
Journal
Biomolecules
ISSN: 2218-273X
Titre abrégé: Biomolecules
Pays: Switzerland
ID NLM: 101596414
Informations de publication
Date de publication:
06 08 2020
06 08 2020
Historique:
received:
16
07
2020
revised:
03
08
2020
accepted:
04
08
2020
entrez:
13
8
2020
pubmed:
13
8
2020
medline:
18
2
2021
Statut:
epublish
Résumé
Many bacteria require ATP binding cassette (ABC) transporters for the import of the essential metal zinc from limited environments. These systems rely on a periplasmic or cell-surface solute binding protein (SBP) to bind zinc with high affinity and specificity. AztABCD is one such zinc transport system recently identified in a large group of diverse bacterial species. In addition to a classical SBP (AztC), the operon also includes a periplasmic metallochaperone (AztD) shown to transfer zinc directly to AztC. Crystal structures of both proteins from
Identifiants
pubmed: 32781785
pii: biom10081156
doi: 10.3390/biom10081156
pmc: PMC7463823
pii:
doi:
Substances chimiques
ATP-Binding Cassette Transporters
0
Bacterial Proteins
0
Cation Transport Proteins
0
Zinc
J41CSQ7QDS
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM122819
Pays : United States
Organisme : Howard Hughes Medical Institute
Pays : United States
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