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
Author
Journal
IF	>30 >20 >10 >5 all

Title	Insights into phosphoethanolamine cellulose synthesis and secretion across the Gram-negative cell envelope.
Journal, issue, pages	Nat Commun, Vol. 15, Issue 1, Page 7798, Year 2024
Publish date	Sep 6, 2024
Authors	Preeti Verma / Ruoya Ho / Schuyler A Chambers / Lynette Cegelski / Jochen Zimmer /
PubMed Abstract	Phosphoethanolamine (pEtN) cellulose is a naturally occurring modified cellulose produced by several Enterobacteriaceae. The minimal components of the E. coli cellulose synthase complex include the ...Phosphoethanolamine (pEtN) cellulose is a naturally occurring modified cellulose produced by several Enterobacteriaceae. The minimal components of the E. coli cellulose synthase complex include the catalytically active BcsA enzyme, a hexameric semicircle of the periplasmic BcsB protein, and the outer membrane (OM)-integrated BcsC subunit containing periplasmic tetratricopeptide repeats (TPR). Additional subunits include BcsG, a membrane-anchored periplasmic pEtN transferase associated with BcsA, and BcsZ, a periplasmic cellulase of unknown biological function. While cellulose synthesis and translocation by BcsA are well described, little is known about its pEtN modification and translocation across the cell envelope. We show that the N-terminal cytosolic domain of BcsA positions three BcsG copies near the nascent cellulose polymer. Further, the semicircle's terminal BcsB subunit tethers the N-terminus of a single BcsC protein in a trans-envelope secretion system. BcsC's TPR motifs bind a putative cello-oligosaccharide near the entrance to its OM pore. Additionally, we show that only the hydrolytic activity of BcsZ but not the subunit itself is necessary for cellulose secretion, suggesting a secretion mechanism based on enzymatic removal of translocation incompetent cellulose. Lastly, protein engineering introduces cellulose pEtN modification in orthogonal cellulose biosynthetic systems. These findings advance our understanding of pEtN cellulose modification and secretion.
External links	Nat Commun / PubMed:39242554 / PubMed Central
Methods	EM (single particle)
Resolution	2.65 - 5.71 Å
Structure data	44334 9b87 EMDB-44334, PDB-9b87: Tetrameric cryo-EM structure of E. coli BcsZ Method: EM (single particle) / Resolution: 2.65 Å 44336 9b8a EMDB-44336, PDB-9b8a: Cryo-EM structure of E. coli cellulose synthase subunit C Method: EM (single particle) / Resolution: 3.4 Å 44345 9b8h EMDB-44345, PDB-9b8h: Cryo-EM structure of E. coli cellulose synthase subunit C with cellotetraose Method: EM (single particle) / Resolution: 3.8 Å 44346 9b8i EMDB-44346, PDB-9b8i: Cryo-EM structure of the E. coli cellulose synthase BcsB-BcsC fusion protein Method: EM (single particle) / Resolution: 3.18 Å 44359 9b8v EMDB-44359: Cryo-EM map of the E. coli cellulose synthase BcsAG3B6 complex PDB-9b8v: AlphaFold2 informed cryo-EM model of the E. coli cellulose synthase BcsAG3B6 complex Method: EM (single particle) / Resolution: 4.0 Å EMDB-44793: E. coli cellulose synthase BcsAG3B6 complex - Consensus map Method: EM (single particle) / Resolution: 5.67 Å EMDB-44794: E. coli cellulose synthase BcsAG3B6 complex - BcsB focused map Method: EM (single particle) / Resolution: 4.0 Å EMDB-44795: E.coli cellulose synthase BcsAG3B6 complex - BcsAG focused map Method: EM (single particle) / Resolution: 5.71 Å
Source	escherichia coli (E. coli)
Keywords	HYDROLASE / Cellulase / Endoglucanase / GH-8 family / Carbohydrate-active enzyme / MEMBRANE PROTEIN / Porin / bacterial outer membrane protein / Tetra-tricopeptide (TPR) repeats / Cellulose exporter BcsC / BcsC outer membrane protein / cellooligosaccharide / STRUCTURAL PROTEIN / bacterial cellulose synthesis / cellulose export / outer membrane porin / periplasmic protein / TRANSFERASE / phosphoethanolamine (pEtN) / catalytic BcsA-B / c-di-GMP binding protein / membrane proteins