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-Structure paper
タイトル | Mechanism of cyclic β-glucan export by ABC transporter Cgt of Brucella. |
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ジャーナル・号・ページ | Nat Struct Mol Biol, Vol. 29, Issue 12, Page 1170-1177, Year 2022 |
掲載日 | 2022年12月1日 |
著者 | Jaroslaw Sedzicki / Dongchun Ni / Frank Lehmann / Na Wu / Renato Zenobi / Seunho Jung / Henning Stahlberg / Christoph Dehio / |
PubMed 要旨 | Polysaccharides play critical roles in bacteria, including the formation of protective capsules and biofilms and establishing specific host cell interactions. Their transport across membranes is ...Polysaccharides play critical roles in bacteria, including the formation of protective capsules and biofilms and establishing specific host cell interactions. Their transport across membranes is often mediated by ATP-binding cassette (ABC) transporters, which utilize ATP to translocate diverse molecules. Cyclic β-glucans (CβGs) are critical for host interaction of the Rhizobiales, including the zoonotic pathogen Brucella. CβGs are exported into the periplasmic space by the cyclic glucan transporter (Cgt). The interaction of an ABC transporter with a polysaccharide substrate has not been visualized so far. Here we use single-particle cryoelectron microscopy to elucidate the structures of Cgt from Brucella abortus in four conformational states. The substrate-bound structure reveals an unusual binding pocket at the height of the cytoplasmic leaflet, whereas ADP-vanadate models hint at an alternative mechanism of substrate release. Our work provides insights into the translocation of large, heterogeneous substrates and sheds light on protein-polysaccharide interactions in general. |
リンク | Nat Struct Mol Biol / PubMed:36456825 |
手法 | EM (単粒子) |
解像度 | 3.5 - 4.0 Å |
構造データ | EMDB-14814, PDB-7znu: EMDB-14843, PDB-7zo8: EMDB-14844, PDB-7zo9: EMDB-14845, PDB-7zoa: |
化合物 | ChemComp-ADP: ChemComp-VO4: ChemComp-PLC: |
由来 |
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キーワード | SUGAR BINDING PROTEIN / cyclic-beta-glucan / ABC transporter / CGT / Brucella |