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-Structure paper
タイトル | Bacterial crystalline cellulose secretion via a supramolecular BcsHD scaffold. |
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ジャーナル・号・ページ | Sci Adv, Vol. 8, Issue 50, Page eadd1170, Year 2022 |
掲載日 | 2022年12月16日 |
著者 | Wiem Abidi / Marion Decossas / Lucía Torres-Sánchez / Lucie Puygrenier / Sylvie Létoffé / Jean-Marc Ghigo / Petya V Krasteva / |
PubMed 要旨 | Cellulose, the most abundant biopolymer on Earth, is not only the predominant constituent of plants but also a key extracellular polysaccharide in the biofilms of many bacterial species. Depending on ...Cellulose, the most abundant biopolymer on Earth, is not only the predominant constituent of plants but also a key extracellular polysaccharide in the biofilms of many bacterial species. Depending on the producers, chemical modifications, and three-dimensional assemblies, bacterial cellulose (BC) can present diverse degrees of crystallinity. Highly ordered, or crystalline, cellulose presents great economical relevance due to its ever-growing number of biotechnological applications. Even if some acetic acid bacteria have long been identified as BC superproducers, the molecular mechanisms determining the secretion of crystalline versus amorphous cellulose remain largely unknown. Here, we present structural and mechanistic insights into the role of the accessory subunits BcsH (CcpAx) and BcsD (CesD) that determine crystalline BC secretion in the lineage. We show that oligomeric BcsH drives the assembly of BcsD into a supramolecular cytoskeletal scaffold that likely stabilizes the cellulose-extruding synthase nanoarrays through an unexpected inside-out mechanism for secretion system assembly. |
リンク | Sci Adv / PubMed:36525496 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.6 - 3.3 Å |
構造データ | EMDB-15039, PDB-7zzq: EMDB-15040: BcsHD cis-filaments: four 'beads-on-a-string' EMDB-15041, PDB-7zzy: |
化合物 | ChemComp-HOH: |
由来 |
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キーワード | STRUCTURAL PROTEIN / Bacterial cytoskeleton / cellulose secretion / Crystalline cellulose secretion |