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TitleStructures and roles of BcsD and partner scaffold proteins in proteobacterial cellulose secretion.
Journal, issue, pagesCurr Biol, Vol. 34, Issue 1, Page 106-116.e6, Year 2024
Publish dateJan 8, 2024
AuthorsThibault G Sana / Areti Notopoulou / Lucie Puygrenier / Marion Decossas / Sandra Moreau / Aurélien Carlier / Petya V Krasteva /
PubMed AbstractCellulose is the world's most abundant biopolymer, and similar to its role as a cell wall component in plants, it is a prevalent constituent of the extracellular matrix in bacterial biofilms. ...Cellulose is the world's most abundant biopolymer, and similar to its role as a cell wall component in plants, it is a prevalent constituent of the extracellular matrix in bacterial biofilms. Although bacterial cellulose (BC) was first described in the 19 century, it was only recently revealed that it is produced by several distinct types of Bcs secretion systems that feature multiple accessory subunits in addition to a catalytic BcsAB synthase tandem. We recently showed that crystalline cellulose secretion in the Gluconacetobacter genus (α-Proteobacteria) is driven by a supramolecular BcsH-BcsD scaffold-the "cortical belt"-which stabilizes the synthase nanoarrays through an unexpected inside-out mechanism for secretion system assembly. Interestingly, while bcsH is specific for Gluconacetobacter, bcsD homologs are widespread in Proteobacteria. Here, we examine BcsD homologs and their gene neighborhoods from several plant-colonizing β- and γ-Proteobacteria proposed to secrete a variety of non-crystalline and/or chemically modified cellulosic polymers. We provide structural and mechanistic evidence that through different quaternary structure assemblies BcsD acts with proline-rich BcsH, BcsP, or BcsO partners across the proteobacterial clade to form synthase-interacting intracellular scaffolds that, in turn, determine the biofilm strength and architecture in species with strikingly different physiology and secreted biopolymers.
External linksCurr Biol / PubMed:38141614
MethodsEM (single particle)
Resolution2.33 - 4.15 Å
Structure data

17735

8pkd

EMDB-17735, PDB-8pkd:
Cryo-EM structure of Orrella dioscoreae BcsD
Method: EM (single particle) / Resolution: 2.33 Å

17788

8poc

EMDB-17788, PDB-8poc:
Cryo-EM structure of Dickeya dadantii BcsD
Method: EM (single particle) / Resolution: 4.0 Å

17791

8pog

EMDB-17791, PDB-8pog:
Cryo-EM structure of Enterobacter sp. 638 BcsD
Method: EM (single particle) / Resolution: 4.15 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • orrella dioscoreae (bacteria)
  • dickeya dadantii 3937 (bacteria)
  • enterobacter sp. 638 (bacteria)
KeywordsSTRUCTURAL PROTEIN / Bacterial cytoskeleton / bacterial cellulose / bacterial secretion / bacterial biofilms / CYTOSOLIC PROTEIN / Cellulose secretion / cytoskeleton

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