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8HPM

LpqY-SugABC in state 2

Summary for 8HPM
Entry DOI10.2210/pdb8hpm/pdb
EMDB information34933
DescriptorABC sugar transporter, permease component, ABC transporter, permease protein SugB, ABC transporter, ATP-binding protein SugC, ... (6 entities in total)
Functional Keywordstrehalose, abc transporter, tuberculosis, transport protein
Biological sourceMycolicibacterium smegmatis MC2 155
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Total number of polymer chains5
Total formula weight201523.69
Authors
Liang, J.,Yang, X.,Zhang, B.,Rao, Z.,Liu, F. (deposition date: 2022-12-12, release date: 2023-09-06, Last modification date: 2023-10-18)
Primary citationLiang, 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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數據於2024-11-06公開中

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