8tsh: Difference between revisions
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==S. thermodepolymerans KpsMT(E151Q)-KpsE in complex with ATP== | |||
<StructureSection load='8tsh' size='340' side='right'caption='[[8tsh]], [[Resolution|resolution]] 3.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8tsh]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Caldimonas_thermodepolymerans Caldimonas thermodepolymerans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8TSH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8TSH 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]] 3.1Å</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=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=8tsh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8tsh OCA], [https://pdbe.org/8tsh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8tsh RCSB], [https://www.ebi.ac.uk/pdbsum/8tsh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8tsh ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A2S5T4B3_9BURK A0A2S5T4B3_9BURK] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Capsular polysaccharides (CPSs) fortify the cell boundaries of many commensal and pathogenic bacteria(1). Through the ABC-transporter-dependent biosynthesis pathway, CPSs are synthesized intracellularly on a lipid anchor and secreted across the cell envelope by the KpsMT ABC transporter associated with the KpsE and KpsD subunits(1,2). Here we use structural and functional studies to uncover crucial steps of CPS secretion in Gram-negative bacteria. We show that KpsMT has broad substrate specificity and is sufficient for the translocation of CPSs across the inner bacterial membrane, and we determine the cell surface organization and localization of CPSs using super-resolution fluorescence microscopy. Cryo-electron microscopy analyses of the KpsMT-KpsE complex in six different states reveal a KpsE-encaged ABC transporter, rigid-body conformational rearrangements of KpsMT during ATP hydrolysis and recognition of a glycolipid inside a membrane-exposed electropositive canyon. In vivo CPS secretion assays underscore the functional importance of canyon-lining basic residues. Combined, our analyses suggest a molecular model of CPS secretion by ABC transporters. | |||
Molecular insights into capsular polysaccharide secretion.,Kuklewicz J, Zimmer J Nature. 2024 Apr;628(8009):901-909. doi: 10.1038/s41586-024-07248-9. Epub 2024 , Apr 3. PMID:38570679<ref>PMID:38570679</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8tsh" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Caldimonas thermodepolymerans]] | |||
[[Category: Large Structures]] | |||
[[Category: Kuklewicz J]] | |||
[[Category: Zimmer J]] | |||
Latest revision as of 15:11, 30 October 2024
S. thermodepolymerans KpsMT(E151Q)-KpsE in complex with ATPS. thermodepolymerans KpsMT(E151Q)-KpsE in complex with ATP
Structural highlights
FunctionPublication Abstract from PubMedCapsular polysaccharides (CPSs) fortify the cell boundaries of many commensal and pathogenic bacteria(1). Through the ABC-transporter-dependent biosynthesis pathway, CPSs are synthesized intracellularly on a lipid anchor and secreted across the cell envelope by the KpsMT ABC transporter associated with the KpsE and KpsD subunits(1,2). Here we use structural and functional studies to uncover crucial steps of CPS secretion in Gram-negative bacteria. We show that KpsMT has broad substrate specificity and is sufficient for the translocation of CPSs across the inner bacterial membrane, and we determine the cell surface organization and localization of CPSs using super-resolution fluorescence microscopy. Cryo-electron microscopy analyses of the KpsMT-KpsE complex in six different states reveal a KpsE-encaged ABC transporter, rigid-body conformational rearrangements of KpsMT during ATP hydrolysis and recognition of a glycolipid inside a membrane-exposed electropositive canyon. In vivo CPS secretion assays underscore the functional importance of canyon-lining basic residues. Combined, our analyses suggest a molecular model of CPS secretion by ABC transporters. Molecular insights into capsular polysaccharide secretion.,Kuklewicz J, Zimmer J Nature. 2024 Apr;628(8009):901-909. doi: 10.1038/s41586-024-07248-9. Epub 2024 , Apr 3. PMID:38570679[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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