8ja8: Difference between revisions
New page: '''Unreleased structure''' The entry 8ja8 is ON HOLD Authors: Zhang, B., Liang, J., Rao, Z. Description: Crystal structure of Mycobacterium tuberculosis LpqY with trehalose bound in a ... |
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The | ==Crystal structure of Mycobacterium tuberculosis LpqY with trehalose bound in a closed liganded form== | ||
<StructureSection load='8ja8' size='340' side='right'caption='[[8ja8]], [[Resolution|resolution]] 1.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8ja8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8JA8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8JA8 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=8ja8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ja8 OCA], [https://pdbe.org/8ja8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ja8 RCSB], [https://www.ebi.ac.uk/pdbsum/8ja8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ja8 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/LPQY_MYCTU LPQY_MYCTU] Part of the ABC transporter complex LpqY-SugA-SugB-SugC, which is highly specific for uptake of trehalose. Involved in the recycling of extracellular trehalose released from trehalose-containing molecules synthesized by M.tuberculosis. Trehalose uptake is essential for virulence (PubMed:21118978). No binding affinity for maltose (PubMed:35775983).<ref>PMID:21118978</ref> <ref>PMID:35775983</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Trehalose plays a crucial role in the survival and virulence of the deadly human pathogen Mycobacterium tuberculosis (Mtb). The type I ATP-binding cassette (ABC) transporter LpqY-SugABC is the sole pathway for trehalose to enter Mtb. The substrate-binding protein, LpqY, which forms a stable complex with the translocator SugABC, recognizes and captures trehalose and its analogues in the periplasmic space, but the precise molecular mechanism for this process is still not well understood. This study reports a 3.02-A cryoelectron microscopy structure of trehalose-bound Mtb LpqY-SugABC in the pretranslocation state, a crystal structure of Mtb LpqY in a closed form with trehalose bound and five crystal structures of Mtb LpqY in complex with different trehalose analogues. These structures, accompanied by substrate-stimulated ATPase activity data, reveal how LpqY recognizes and binds trehalose and its analogues, and highlight the flexibility in the substrate binding pocket of LpqY. These data provide critical insights into the design of trehalose analogues that could serve as potential molecular probe tools or as anti-TB drugs. | |||
Molecular recognition of trehalose and trehalose analogues by Mycobacterium tuberculosis LpqY-SugABC.,Liang J, Liu F, Xu P, Shangguan W, Hu T, Wang S, Yang X, Xiong Z, Yang X, Guddat LW, Yu B, Rao Z, Zhang B Proc Natl Acad Sci U S A. 2023 Aug 29;120(35):e2307625120. doi: , 10.1073/pnas.2307625120. Epub 2023 Aug 21. PMID:37603751<ref>PMID:37603751</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 8ja8" style="background-color:#fffaf0;"></div> | ||
[[Category: Liang | == References == | ||
[[Category: Rao | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mycobacterium tuberculosis H37Rv]] | |||
[[Category: Liang J]] | |||
[[Category: Rao Z]] | |||
[[Category: Zhang B]] | |||
Latest revision as of 15:04, 30 October 2024
Crystal structure of Mycobacterium tuberculosis LpqY with trehalose bound in a closed liganded formCrystal structure of Mycobacterium tuberculosis LpqY with trehalose bound in a closed liganded form
Structural highlights
FunctionLPQY_MYCTU Part of the ABC transporter complex LpqY-SugA-SugB-SugC, which is highly specific for uptake of trehalose. Involved in the recycling of extracellular trehalose released from trehalose-containing molecules synthesized by M.tuberculosis. Trehalose uptake is essential for virulence (PubMed:21118978). No binding affinity for maltose (PubMed:35775983).[1] [2] Publication Abstract from PubMedTrehalose plays a crucial role in the survival and virulence of the deadly human pathogen Mycobacterium tuberculosis (Mtb). The type I ATP-binding cassette (ABC) transporter LpqY-SugABC is the sole pathway for trehalose to enter Mtb. The substrate-binding protein, LpqY, which forms a stable complex with the translocator SugABC, recognizes and captures trehalose and its analogues in the periplasmic space, but the precise molecular mechanism for this process is still not well understood. This study reports a 3.02-A cryoelectron microscopy structure of trehalose-bound Mtb LpqY-SugABC in the pretranslocation state, a crystal structure of Mtb LpqY in a closed form with trehalose bound and five crystal structures of Mtb LpqY in complex with different trehalose analogues. These structures, accompanied by substrate-stimulated ATPase activity data, reveal how LpqY recognizes and binds trehalose and its analogues, and highlight the flexibility in the substrate binding pocket of LpqY. These data provide critical insights into the design of trehalose analogues that could serve as potential molecular probe tools or as anti-TB drugs. Molecular recognition of trehalose and trehalose analogues by Mycobacterium tuberculosis LpqY-SugABC.,Liang J, Liu F, Xu P, Shangguan W, Hu T, Wang S, Yang X, Xiong Z, Yang X, Guddat LW, Yu B, Rao Z, Zhang B Proc Natl Acad Sci U S A. 2023 Aug 29;120(35):e2307625120. doi: , 10.1073/pnas.2307625120. Epub 2023 Aug 21. PMID:37603751[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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