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	Structural insights into the transition of Clostridioides difficile binary toxin from prepore to pore.
Journal, issue, pages	Nat Microbiol, Vol. 5, Issue 1, Page 102-107, Year 2020
Publish date	Nov 11, 2019
Authors	David M Anderson / Michael J Sheedlo / Jaime L Jensen / D Borden Lacy /
PubMed Abstract	Clostridioides (formerly Clostridium) difficile is a Gram-positive, spore-forming anaerobe and a leading cause of hospital-acquired infection and gastroenteritis-associated death in US hospitals. The ...Clostridioides (formerly Clostridium) difficile is a Gram-positive, spore-forming anaerobe and a leading cause of hospital-acquired infection and gastroenteritis-associated death in US hospitals. The disease state is usually preceded by disruption of the host microbiome in response to antibiotic treatment and is characterized by mild to severe diarrhoea. C. difficile infection is dependent on the secretion of one or more AB-type toxins: toxin A (TcdA), toxin B (TcdB) and the C. difficile transferase toxin (CDT). Whereas TcdA and TcdB are considered the primary virulence factors, recent studies suggest that CDT increases the severity of C. difficile infection in some of the most problematic clinical strains. To better understand how CDT functions, we used cryo-electron microscopy to define the structure of CDTb, the cell-binding component of CDT. We obtained structures of several oligomeric forms that highlight the conformational changes that enable conversion from a prepore to a β-barrel pore. The structural analysis also reveals a glycan-binding domain and residues involved in binding the host-cell receptor, lipolysis-stimulated lipoprotein receptor. Together, these results provide a framework to understand how CDT functions at the host cell interface.
External links	Nat Microbiol / PubMed:31712627 / PubMed Central
Methods	EM (single particle)
Resolution	3.7 - 6.3 Å
Structure data	0608 6o2m EMDB-0608: Reconstruction of CDTb Double Heptamer Long Form using C7 Symmetry PDB-6o2m: CDTb Double Heptamer Long Form Modeled from Cryo-EM Map Reconstructed using C7 Symmetry Method: EM (single particle) / Resolution: 6.3 Å 0609 6o2n EMDB-0609: Reconstruction of CDTb Double Heptamer Short Form using C7 Symmetry PDB-6o2n: CDTb Double Heptamer Short Form Modeled from Cryo-EM Map Reconstructed using C7 Symmetry Method: EM (single particle) / Resolution: 3.7 Å 0610 6o2o EMDB-0610: Reconstruction of CDTb Double Heptamer Short Form using C1 Symmetry PDB-6o2o: CDTb Double Heptamer Short Form Modeled from Cryo-EM Map Reconstructed using C1 Symmetry Method: EM (single particle) / Resolution: 4.53 Å 20102 6okr EMDB-20102, PDB-6okr: CDTb Pre-Insertion form Modeled from Cryo-EM Map Reconstructed using C7 Symmetry Method: EM (single particle) / Resolution: 4.2 Å 20103 6oks EMDB-20103, PDB-6oks: CDTb Double Heptamer Long Form Mask 1 Modeled from Cryo-EM Map Reconstructed using C7 Symmetry Method: EM (single particle) / Resolution: 4.2 Å 20104 6okt EMDB-20104, PDB-6okt: CDTb Double Heptamer Long Form Mask 1 Modeled from Cryo-EM Map Reconstructed using C7 Symmetry Method: EM (single particle) / Resolution: 4.2 Å 20105 6oku EMDB-20105, PDB-6oku: CDTb Double Heptamer Long Form Mask 3 Modeled from Cryo-EM Map Reconstructed using C7 Symmetry Method: EM (single particle) / Resolution: 3.8 Å
Source	clostridioides difficile (bacteria)
Keywords	TRANSFERASE / CDTb / Clostridium / Toxin / Binary / difficil / difficile