Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
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Journal
IF	>30 >20 >10 >5 all

Title	Structural basis for synthase activation and cellulose modification in the E. coli Type II Bcs secretion system.
Journal, issue, pages	Nat Commun, Vol. 15, Issue 1, Page 8799, Year 2024
Publish date	Oct 11, 2024
Authors	Itxaso Anso / Samira Zouhir / Thibault Géry Sana / Petya Violinova Krasteva /
PubMed Abstract	Bacterial cellulosic polymers constitute a prevalent class of biofilm matrix exopolysaccharides that are synthesized by several types of bacterial cellulose secretion (Bcs) systems, which include ...Bacterial cellulosic polymers constitute a prevalent class of biofilm matrix exopolysaccharides that are synthesized by several types of bacterial cellulose secretion (Bcs) systems, which include conserved cyclic diguanylate (c-di-GMP)-dependent cellulose synthase modules together with diverse accessory subunits. In E. coli, the biogenesis of phosphoethanolamine (pEtN)-modified cellulose relies on the BcsRQABEFG macrocomplex, encompassing inner-membrane and cytosolic subunits, and an outer membrane porin, BcsC. Here, we use cryogenic electron microscopy to shed light on the molecular mechanisms of BcsA-dependent recruitment and stabilization of a trimeric BcsG pEtN-transferase for polymer modification, and a dimeric BcsF-dependent recruitment of an otherwise cytosolic BcsERQ regulatory complex. We further demonstrate that BcsE, a secondary c-di-GMP sensor, can remain dinucleotide-bound and retain the essential-for-secretion BcsRQ partners onto the synthase even in the absence of direct c-di-GMP-synthase complexation, likely lowering the threshold for c-di-GMP-dependent synthase activation. Such activation-by-proxy mechanism could allow Bcs secretion system activity even in the absence of substantial intracellular c-di-GMP increase, and is reminiscent of other widespread synthase-dependent polysaccharide secretion systems where dinucleotide sensing and/or synthase stabilization are carried out by key co-polymerase subunits.
External links	Nat Commun / PubMed:39394223 / PubMed Central
Methods	EM (single particle)
Resolution	2.35 - 7.0 Å
Structure data	50567 9fmt EMDB-50567, PDB-9fmt: Cryo-EM structure of the BcsB hexameric crown from the E. coli cellulose secretion macrocomplex Method: EM (single particle) / Resolution: 2.35 Å 50571 9fmv EMDB-50571, PDB-9fmv: Cryo-EM structure of the c-di-GMP-free synthase:pEtN transferase complex (BcsA-Bct-G3) from the E. coli cellulose secretion macrocomplex Method: EM (single particle) / Resolution: 3.43 Å 50581 9fmz EMDB-50581, PDB-9fmz: Cryo-EM structure of the c-di-GMP-bound synthase:pEtN transferase complex (BcsA-Bct-G3) from the E. coli cellulose secretion macrocomplex Method: EM (single particle) / Resolution: 3.6 Å EMDB-50584: Cryo-EM structure of the c-di-GMP-saturated Bcs macrocomplex (BcsABR2Q2E2F2G3) for cellulose secretion of E. coli (filtered to 6A) Method: EM (single particle) / Resolution: 6.0 Å EMDB-50595: Cryo-EM structure of the c-di-GMP non-saturated Bcs macrocomplex (BcsABR2Q2E2F2G3) for cellulose secretion of E. coli (filtered to 7A) Method: EM (single particle) / Resolution: 7.0 Å 50599 9fnn EMDB-50599, PDB-9fnn: Cryo-EM structure of the c-di-GMP-saturated 'crown'less Bcs macrocomplex for cellulose secretion in E. coli Method: EM (single particle) / Resolution: 2.85 Å 50619 9fo7 EMDB-50619, PDB-9fo7: Cryo-EM structure of the BcsE2F2 regulatory subcomplex from the E. coli Bcs macrocomplex for cellulose secretion (local refinement) Method: EM (single particle) / Resolution: 2.85 Å 50632 9fp0 EMDB-50632, PDB-9fp0: Cryo-EM structure of the 'crown'less Bcs macrocomplex for E. coli cellulose secretion in non-saturating c-di-GMP (local) Method: EM (single particle) / Resolution: 3.37 Å 50633 9fp2 EMDB-50633, PDB-9fp2: Cryo-EM structure of the BcsEFRQ regulatory subcomplex for E. coli cellulose secretion in non-saturating c-di-GMP (local) Method: EM (single particle) / Resolution: 3.76 Å
Chemicals	ChemComp-C2E: 9,9'-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one) ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM ChemComp-MG*: Unknown entry
Source	escherichia coli (E. coli)
Keywords	MEMBRANE PROTEIN / Bacterial cellulose secretion