7ZZQ

BcsH-BcsD 'beads-on-a-string' filament, local refine

7ZZQ の概要

• エントリーDOI: 10.2210/pdb7zzq/pdb
• EMDBエントリー: 15039 15040 15041
• 分子名称: Cellulose biosynthesis protein, BcsH fragment (3 entities in total)
• 機能のキーワード: bacterial cytoskeleton, cellulose secretion, structural protein
• 由来する生物種: Komagataeibacter hansenii ATCC 23769; 詳細
• タンパク質・核酸の鎖数: 30
• 化学式量合計: 434632.39

構造登録者

Krasteva, P.V.,Abidi, W.,Decossas, M. (登録日: 2022-05-26, 公開日: 2022-12-28, 最終更新日: 2025-07-09)

主引用文献

Abidi, W.,Decossas, M.,Torres-Sanchez, L.,Puygrenier, L.,Letoffe, S.,Ghigo, J.M.,Krasteva, P.V.
Bacterial crystalline cellulose secretion via a supramolecular BcsHD scaffold.
Sci Adv, 8:eadd1170-eadd1170, 2022

PubMed Abstract: 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.

PubMed: 36525496
DOI: 10.1126/sciadv.add1170

実験手法

ELECTRON MICROSCOPY (2.6 Å)