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-Structure paper
タイトル | Conformational snapshots of the bacitracin sensing and resistance transporter BceAB. |
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ジャーナル・号・ページ | Proc Natl Acad Sci U S A, Vol. 119, Issue 14, Page e2123268119, Year 2022 |
掲載日 | 2022年4月5日 |
著者 | Natasha L George / Anthony L Schilmiller / Benjamin J Orlando / |
PubMed 要旨 | SignificanceMany gram-positive organisms have evolved an elegant solution to sense and resist antimicrobial peptides that inhibit cell-wall synthesis. These organisms express an unusual "Bce-type" ...SignificanceMany gram-positive organisms have evolved an elegant solution to sense and resist antimicrobial peptides that inhibit cell-wall synthesis. These organisms express an unusual "Bce-type" adenosine triphosphate-binding cassette (ABC) transporter that recognizes complexes formed between antimicrobial peptides and lipids involved in cell-wall biosynthesis. In this work, we provide the first structural snapshots of a Bce-type ABC transporter trapped in different conformational states. Our structures and associated biochemical data provide key insights into the novel target protection mechanism that these unusual ABC transporters use to sense and resist antimicrobial peptides. The studies described herein set the stage to begin developing a comprehensive molecular understanding of the diverse interactions between antimicrobial peptides and conserved resistance machinery found across most gram-positive organisms. |
リンク | Proc Natl Acad Sci U S A / PubMed:35349335 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.7 - 3.8 Å |
構造データ | EMDB-25811, PDB-7tcg: EMDB-25812, PDB-7tch: |
化合物 | ChemComp-I0O: ChemComp-ATP: |
由来 |
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キーワード | TRANSPORT PROTEIN / BceAB / bacitracin / transporter |