8hps: Difference between revisions
New page: '''Unreleased structure''' The entry 8hps is ON HOLD Authors: Liang, J., Yang, X., Zhang, B., Rao, Z., Liu, F. Description: LpqY-SugABC in catalytic intermediate state [[Category: Unre... |
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The | ==LpqY-SugABC in state 5== | ||
<StructureSection load='8hps' size='340' side='right'caption='[[8hps]], [[Resolution|resolution]] 3.51Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8hps]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis_MC2_155 Mycolicibacterium smegmatis MC2 155]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HPS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HPS FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.51Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=8hps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hps OCA], [https://pdbe.org/8hps PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hps RCSB], [https://www.ebi.ac.uk/pdbsum/8hps PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hps ProSAT]</span></td></tr> | |||
</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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 8hps" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: Liu | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Mycolicibacterium smegmatis MC2 155]] | |||
[[Category: Liang J]] | |||
[[Category: Liu F]] | |||
[[Category: Rao Z]] | |||
[[Category: Yang X]] | |||
[[Category: Zhang B]] | |||
Latest revision as of 09:24, 6 September 2023
LpqY-SugABC in state 5LpqY-SugABC in state 5
Structural highlights
FunctionPublication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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