7ZZQ

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

Summary for 7ZZQ

• Entry DOI: 10.2210/pdb7zzq/pdb
• EMDB information: 15039 15040 15041
• Descriptor: Cellulose biosynthesis protein, BcsH fragment (3 entities in total)
• Functional Keywords: bacterial cytoskeleton, cellulose secretion, structural protein
• Biological source: Komagataeibacter hansenii ATCC 23769; More
• Total number of polymer chains: 30
• Total formula weight: 434632.39

Authors

Krasteva, P.V.,Abidi, W.,Decossas, M. (deposition date: 2022-05-26, release date: 2022-12-28, Last modification date: 2025-07-09)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (2.6 Å)