7b0k: Difference between revisions
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==membrane protein structure== | ==membrane protein structure== | ||
<StructureSection load='7b0k' size='340' side='right'caption='[[7b0k]]' scene=''> | <StructureSection load='7b0k' size='340' side='right'caption='[[7b0k]], [[Resolution|resolution]] 3.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7B0K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7B0K FirstGlance]. <br> | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7B0K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7B0K FirstGlance]. <br> | ||
</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=7b0k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7b0k OCA], [https://pdbe.org/7b0k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7b0k RCSB], [https://www.ebi.ac.uk/pdbsum/7b0k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7b0k ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.8Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CHT:CHOLINE+ION'>CHT</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=7b0k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7b0k OCA], [https://pdbe.org/7b0k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7b0k RCSB], [https://www.ebi.ac.uk/pdbsum/7b0k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7b0k ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Phosphocholine molecules decorating bacterial cell wall teichoic acids and outer-membrane lipopolysaccharide have fundamental roles in adhesion to host cells, immune evasion, and persistence. Bacteria carrying the operon that performs phosphocholine decoration synthesize phosphocholine after uptake of the choline precursor by LicB, a conserved transporter among divergent species. Streptococcus pneumoniae is a prominent pathogen where phosphocholine decoration plays a fundamental role in virulence. Here, we present cryo-electron microscopy and crystal structures of S. pneumoniae LicB, revealing distinct conformational states and describing architectural and mechanistic elements essential to choline import. Together with in vitro and in vivo functional characterization, we found that LicB displays proton-coupled import activity and promiscuous selectivity involved in adaptation to choline deprivation conditions, and describe LicB inhibition by synthetic nanobodies (sybodies). Our results provide previously unknown insights into the molecular mechanism of a key transporter involved in bacterial pathogenesis and establish a basis for inhibition of the phosphocholine modification pathway across bacterial phyla. | |||
Mechanistic basis of choline import involved in teichoic acids and lipopolysaccharide modification.,Barland N, Rueff AS, Cebrero G, Hutter CAJ, Seeger MA, Veening JW, Perez C Sci Adv. 2022 Mar 4;8(9):eabm1122. doi: 10.1126/sciadv.abm1122. Epub 2022 Mar 2. PMID:35235350<ref>PMID:35235350</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7b0k" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
