6X6L
Cryo-EM Structure of CagX and CagY within the dCag3 Helicobacter pylori PR
This is a non-PDB format compatible entry.
Summary for 6X6L
Entry DOI | 10.2210/pdb6x6l/pdb |
EMDB information | 22077 |
Descriptor | Cag pathogenicity island protein (Cag8), Cag pathogenicity island protein (Cag7) (2 entities in total) |
Functional Keywords | t4ss, secretion, protein transport |
Biological source | Helicobacter pylori (strain ATCC 700392 / 26695) More |
Total number of polymer chains | 34 |
Total formula weight | 4766051.41 |
Authors | Sheedlo, M.J.,Chung, J.M.,Sawhney, N.,Durie, C.L.,Cover, T.L.,Ohi, M.D.,Lacy, D.B. (deposition date: 2020-05-28, release date: 2020-09-30, Last modification date: 2024-10-09) |
Primary citation | Sheedlo, M.J.,Chung, J.M.,Sawhney, N.,Durie, C.L.,Cover, T.L.,Ohi, M.D.,Lacy, D.B. Cryo-EM reveals species-specific components within the Helicobacter pylori Cag type IV secretion system core complex. Elife, 9:-, 2020 Cited by PubMed Abstract: The pathogenesis of -associated gastric cancer is dependent on delivery of CagA into host cells through a type IV secretion system (T4SS). The Cag T4SS includes a large membrane-spanning core complex containing five proteins, organized into an outer membrane cap (OMC), a periplasmic ring (PR) and a stalk. Here, we report cryo-EM reconstructions of a core complex lacking Cag3 and an improved map of the wild-type complex. We define the structures of two unique species-specific components (Cag3 and CagM) and show that Cag3 is structurally similar to CagT. Unexpectedly, components of the OMC are organized in a 1:1:2:2:5 molar ratio (CagY:CagX:CagT:CagM:Cag3). CagX and CagY are components of both the OMC and the PR and bridge the symmetry mismatch between these regions. These results reveal that assembly of the T4SS core complex is dependent on incorporation of interwoven species-specific components. PubMed: 32876048DOI: 10.7554/eLife.59495 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3 Å) |
Structure validation
Download full validation report