8hpr
From Proteopedia
(Difference between revisions)
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8hpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hpr OCA], [https://pdbe.org/8hpr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hpr RCSB], [https://www.ebi.ac.uk/pdbsum/8hpr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hpr ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8hpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hpr OCA], [https://pdbe.org/8hpr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hpr RCSB], [https://www.ebi.ac.uk/pdbsum/8hpr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hpr ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | == Function == | ||
| - | [https://www.uniprot.org/uniprot/I7G6S2_MYCS2 I7G6S2_MYCS2] | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 8hpr" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
LpqY-SugABC in state 4
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