7CAD

Mycobacterium smegmatis SugABC complex

Summary for 7CAD

• Entry DOI: 10.2210/pdb7cad/pdb
• EMDB information: 30327
• Descriptor: ABC transporter, ATP-binding protein SugC, ABC sugar transporter, permease component, ABC transporter, permease protein SugB (3 entities in total)
• Functional Keywords: abc transporter, lipoprotein, mycobacteria, transport protein
• Biological source: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155); More
• Total number of polymer chains: 4
• Total formula weight: 149985.91

Authors

Liu, F.,Liang, J.,Zhang, B.,Gao, Y.,Yang, X.,Hu, T.,Rao, Z. (deposition date: 2020-06-08, release date: 2020-12-02, Last modification date: 2024-03-27)

Primary citation

Liu, 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

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

Experimental method

ELECTRON MICROSCOPY (3.41 Å)