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-Structure paper
タイトル | Mechanistic basis of choline import involved in teichoic acids and lipopolysaccharide modification. |
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ジャーナル・号・ページ | Sci Adv, Vol. 8, Issue 9, Page eabm1122, Year 2022 |
掲載日 | 2022年3月4日 |
![]() | Natalie Bärland / Anne-Stéphanie Rueff / Gonzalo Cebrero / Cedric A J Hutter / Markus A Seeger / Jan-Willem Veening / Camilo Perez / ![]() |
PubMed 要旨 | Phosphocholine molecules decorating bacterial cell wall teichoic acids and outer-membrane lipopolysaccharide have fundamental roles in adhesion to host cells, immune evasion, and persistence. ...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. is a prominent pathogen where phosphocholine decoration plays a fundamental role in virulence. Here, we present cryo-electron microscopy and crystal structures of 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. |
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手法 | EM (単粒子) / X線回折 |
解像度 | 3.75 - 3.8 Å |
構造データ | EMDB-13268, PDB-7paf: ![]() PDB-7b0k: |
化合物 | ![]() ChemComp-CHT: ![]() ChemComp-PGT: |
由来 |
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![]() | TRANSPORT PROTEIN / choline transporter / Importer / Choline / nanodisc / Nanobody |