8HPM
LpqY-SugABC in state 2
Summary for 8HPM
| Entry DOI | 10.2210/pdb8hpm/pdb | 
| EMDB information | 34933 | 
| Descriptor | ABC sugar transporter, permease component, ABC transporter, permease protein SugB, ABC transporter, ATP-binding protein SugC, ... (6 entities in total) | 
| Functional Keywords | trehalose, abc transporter, tuberculosis, transport protein | 
| Biological source | Mycolicibacterium smegmatis MC2 155 More | 
| Total number of polymer chains | 5 | 
| Total formula weight | 201523.69 | 
| Authors | |
| Primary citation | Liang, J.,Yang, X.,Hu, T.,Gao, Y.,Yang, Q.,Yang, H.,Peng, W.,Zhou, X.,Guddat, L.W.,Zhang, B.,Rao, Z.,Liu, F. Structural insights into trehalose capture and translocation by mycobacterial LpqY-SugABC. Structure, 31:1158-1165.e3, 2023 Cited by  PubMed Abstract: The human pathogen, Mycobacterium tuberculosis (Mtb) relies heavily on trehalose for both survival and pathogenicity. The type I ATP-binding cassette (ABC) transporter LpqY-SugABC is the only trehalose import pathway in Mtb. Conformational dynamics of ABC transporters is an important feature to explain how they operate, but experimental structures are determined in a static environment. Therefore, a detailed transport mechanism cannot be elucidated because there is a lack of intermediate structures. Here, we used single-particle cryo-electron microscopy (cryo-EM) to determine the structure of the Mycobacterium smegmatis (M. smegmatis) trehalose-specific importer LpqY-SugABC complex in five different conformations. These structures have been classified and reconstructed from a single cryo-EM dataset. This study allows a comprehensive understanding of the trehalose recycling mechanism in Mycobacteria and also demonstrates the potential of single-particle cryo-EM to explore the dynamic structures of other ABC transporters and molecular machines.PubMed: 37619560 DOI: 10.1016/j.str.2023.07.014 PDB entries with the same primary citation | 
| Experimental method | ELECTRON MICROSCOPY (3.82 Å) | 
Structure validation
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