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7CAG

Mycobacterium smegmatis LpqY-SugABC complex in the catalytic intermediate state

Summary for 7CAG
Entry DOI10.2210/pdb7cag/pdb
EMDB information30330
Related PRD IDPRD_900006
DescriptorBacterial extracellular solute-binding protein, ABC sugar transporter, permease component, ABC transporter, permease protein SugB, ... (7 entities in total)
Functional Keywordsabc transporter, lipoprotein, trehalose, trehalose-specific importer, mycobacteria, transport protein
Biological sourceMycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
More
Total number of polymer chains5
Total formula weight201572.30
Authors
Liu, F.,Liang, J.,Zhang, B.,Gao, Y.,Yang, X.,Hu, T. (deposition date: 2020-06-08, release date: 2020-12-02, Last modification date: 2024-03-27)
Primary citationLiu, F.,Liang, J.,Zhang, B.,Gao, Y.,Yang, X.,Hu, T.,Yang, H.,Xu, W.,Guddat, L.W.,Rao, Z.
Structural basis of trehalose recycling by the ABC transporter LpqY-SugABC.
Sci Adv, 6:-, 2020
Cited by
PubMed Abstract: In bacteria, adenosine 5'-triphosphate (ATP)-binding cassette (ABC) importers are essential for the uptake of nutrients including the nonreducing disaccharide trehalose, a metabolite that is crucial for the survival and virulence of several human pathogens including SugABC is an ABC transporter that translocates trehalose from the periplasmic lipoprotein LpqY into the cytoplasm of mycobacteria. Here, we report four high-resolution cryo-electron microscopy structures of the mycobacterial LpqY-SugABC complex to reveal how it binds and passes trehalose through the membrane to the cytoplasm. A unique feature observed in this system is the initial mode of capture of the trehalose at the LpqY interface. Uptake is achieved by a pivotal rotation of LpqY relative to SugABC, moving from an open and accessible conformation to a clamped conformation upon trehalose binding. These findings enrich our understanding as to how ABC transporters facilitate substrate transport across the membrane in Gram-positive bacteria.
PubMed: 33127676
DOI: 10.1126/sciadv.abb9833
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.78 Å)
Structure validation

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