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7ape

From Proteopedia

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Current revision (07:45, 1 May 2024) (edit) (undo)
 
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<StructureSection load='7ape' size='340' side='right'caption='[[7ape]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='7ape' size='340' side='right'caption='[[7ape]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7ape]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_19527 Atcc 19527]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7APE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7APE FirstGlance]. <br>
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<table><tr><td colspan='2'>[[7ape]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_thermoresistibile Mycolicibacterium thermoresistibile]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7APE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7APE FirstGlance]. <br>
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</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></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RMCT_2827 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1797 ATCC 19527])</td></tr>
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<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=PRD_900006:trehalose'>PRD_900006</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=7ape FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ape OCA], [https://pdbe.org/7ape PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ape RCSB], [https://www.ebi.ac.uk/pdbsum/7ape PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ape 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=7ape FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ape OCA], [https://pdbe.org/7ape PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ape RCSB], [https://www.ebi.ac.uk/pdbsum/7ape PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ape ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/G7CES0_MYCT3 G7CES0_MYCT3]
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The Mycobacterium tuberculosis (Mtb) LpqY-SugABC ATP-binding cassette transporter is a recycling system that imports trehalose released during remodelling of the Mtb cell-envelope. As this process is essential for the virulence of the Mtb pathogen it may represent an important target for tuberculosis drug and diagnostic development, but the transporter specificity and molecular determinants of substrate recognition are unknown. To address this, we have determined the structural and biochemical basis of how mycobacteria transport trehalose using a combination of crystallography, STD NMR, molecular dynamics, site-directed mutagenesis, biochemical/biophysical assays and the synthesis of trehalose analogues. This analysis pinpoints key residues of the LpqY substrate binding lipoprotein that dictate substrate-specific recognition and has revealed which disaccharide modifications are tolerated. These findings provide critical insights into how the essential Mtb LpqY-SugABC transporter reuses trehalose and modified analogues, and specifies a framework that can be exploited for the design of new anti-tubercular agents and/or diagnostic tools.
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Structural basis of trehalose recognition by the mycobacterial LpqY-SugABC transporter.,Furze CM, Delso I, Casal E, Guy CS, Seddon C, Brown CM, Parker HL, Radhakrishnan A, Pacheco-Gomez R, Stansfeld PJ, Angulo J, Cameron AD, Fullam E J Biol Chem. 2021 Jan 18:100307. doi: 10.1016/j.jbc.2021.100307. PMID:33476646<ref>PMID:33476646</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 7ape" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 19527]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Angula, J]]
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[[Category: Mycolicibacterium thermoresistibile]]
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[[Category: Cameron, A D]]
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[[Category: Angula J]]
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[[Category: Fullam, E]]
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[[Category: Cameron AD]]
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[[Category: Furze, C M]]
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[[Category: Fullam E]]
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[[Category: Guy, C M]]
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[[Category: Furze CM]]
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[[Category: Abc-transporter]]
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[[Category: Guy CM]]
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[[Category: Lpqy]]
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[[Category: Transport protein]]
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[[Category: Trehalose complex]]
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[[Category: Tuberculosis]]
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Current revision

Crystal structure of LpqY from Mycobacterium thermoresistible in complex with trehalose

PDB ID 7ape

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