7CAF
Mycobacterium smegmatis LpqY-SugABC complex in the pre-translocation state
Summary for 7CAF
| Entry DOI | 10.2210/pdb7caf/pdb |
| EMDB information | 30329 |
| Related PRD ID | PRD_900006 |
| Descriptor | Bacterial extracellular solute-binding protein, ABC transporter, ATP-binding protein SugC, ABC sugar transporter, permease component, ... (5 entities in total) |
| Functional Keywords | abc transporter, lipoprotein, trehalose, trehalose-specific importer, mycobacteria, transport protein |
| Biological source | Mycolicibacterium smegmatis MC2 155 More |
| Total number of polymer chains | 5 |
| Total formula weight | 200509.32 |
| Authors | |
| 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 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: 33127676DOI: 10.1126/sciadv.abb9833 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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