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An oligopeptide permease, OppABCD, requires an iron–sulfur cluster domain for functionality
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Journal Article
An oligopeptide permease, OppABCD, requires an iron–sulfur cluster domain for functionality
2024
Overview
Oligopeptide permease, OppABCD, belongs to the type I ABC transporter family. Its role is to import oligopeptides into bacteria for nutrient uptake and to modulate the host immune response. OppABCD consists of a cluster C substrate-binding protein (SBP), OppA, membrane-spanning OppB and OppC subunits, and an ATPase, OppD, that contains two nucleotide-binding domains (NBDs). Here, using cryo-electron microscopy, we determined the high-resolution structures of
Mycobacterium tuberculosis
OppABCD in the resting state, oligopeptide-bound pre-translocation state, AMPPNP-bound pre-catalytic intermediate state and ATP-bound catalytic intermediate state. The structures show an assembly of a cluster C SBP with its ABC translocator and a functionally required [4Fe–4S] cluster-binding domain in OppD. Moreover, the ATP-bound OppABCD structure has an outward-occluded conformation, although no substrate was observed in the transmembrane cavity. Here, we reveal an oligopeptide recognition and translocation mechanism of OppABCD, which provides a perspective on how this and other type I ABC importers facilitate bulk substrate transfer across the lipid bilayer.
Here, four cryo-EM structures of
Mtb
OppABCD reveal an assembly of a cluster C substrate-binding protein and its translocator, as well as the [4Fe–4S] cluster-regulated transport mechanism of oligopeptide permeases found in bacteria.
Publisher
Nature Publishing Group US,Nature Publishing Group
Subject
/ Adenosine Triphosphate - metabolism
/ Assembly
/ ATP-Binding Cassette Transporters - chemistry
/ ATP-Binding Cassette Transporters - metabolism
/ Bacteria
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - metabolism
/ Biomedical and Life Sciences
/ Clusters
/ Iron-Sulfur Proteins - chemistry
/ Iron-Sulfur Proteins - metabolism
/ Lipids
/ Membrane Transport Proteins - chemistry
/ Membrane Transport Proteins - metabolism
/ Mycobacterium tuberculosis - enzymology
/ Mycobacterium tuberculosis - metabolism
/ Peptides
/ Permease
/ Proteins
/ Sulfur
