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| </table> | | </table> |
| == Function == | | == Function == |
| [https://www.uniprot.org/uniprot/I7G6S2_MYCS2 I7G6S2_MYCS2] | | [https://www.uniprot.org/uniprot/A0R2C2_MYCS2 A0R2C2_MYCS2] |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| 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.
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| Structural insights into trehalose capture and translocation by mycobacterial LpqY-SugABC.,Liang J, Yang X, Hu T, Gao Y, Yang Q, Yang H, Peng W, Zhou X, Guddat LW, Zhang B, Rao Z, Liu F Structure. 2023 Aug 10:S0969-2126(23)00276-9. doi: 10.1016/j.str.2023.07.014. PMID:37619560<ref>PMID:37619560</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 8hps" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
