EMD-35990

Single-particle
3.25 Å
EMD-35990 Deposition: 24/04/2023
Map released: 03/04/2024
Last modified: 31/07/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-35990

Cryo-EM structure of Mycobacterium tuberculosis OppABCD in the pre-translocation state

EMD-35990

Single-particle
3.25 Å
EMD-35990 Deposition: 24/04/2023
Map released: 03/04/2024
Last modified: 31/07/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv), Mycolicibacterium smegmatis MC2 155
Sample: Cryo-EM structure of Mycobacterium tuberculosis OppABCD in the pre-translocation state
Fitted models: 8j5q (Avg. Q-score: 0.519)

Deposition Authors: Yang X , Hu T, Zhang B , Rao Z
An oligopeptide permease, OppABCD, requires an iron-sulfur cluster domain for functionality.
Yang X , Hu T, Liang J, Xiong Z, Lin Z, Zhao Y , Zhou X, Gao Y , Sun S, Yang X , Guddat LW , Yang H , Rao Z , Zhang B
(2024) Nat Struct Mol Biol , 31 , 1072 - 1082
PUBMED: 38548954
DOI: doi:10.1038/s41594-024-01256-z
ISSN: 1545-9985
Abstract:
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.