7OVB
L. pneumophila Type IV Coupling Complex (T4CC) with density for DotY N-terminal and middle domains
Summary for 7OVB
| Entry DOI | 10.2210/pdb7ovb/pdb |
| EMDB information | 13083 |
| Descriptor | IcmO (DotL), IcmP (DotM), IcmJ (DotN), ... (6 entities in total) |
| Functional Keywords | type iv coupling complex, t4cc, type iv secretion system, t4ss, membrane protein complex, membrane complex, doty, dotz, dotl, dotm, dotn, icmsw, legionella, membrane protein |
| Biological source | Legionella pneumophila subsp. pneumophila str. Philadelphia 1 More |
| Total number of polymer chains | 5 |
| Total formula weight | 214726.72 |
| Authors | Mace, K.,Meir, A.,Lukoyanova, N.,Waksman, G. (deposition date: 2021-06-14, release date: 2021-12-01, Last modification date: 2024-07-17) |
| Primary citation | Mace, K.,Meir, A.,Lukoyanova, N.,Liu, L.,Chetrit, D.,Hospenthal, M.K.,Roy, C.R.,Waksman, G. Proteins DotY and DotZ modulate the dynamics and localization of the type IVB coupling complex of Legionella pneumophila. Mol.Microbiol., 117:307-319, 2022 Cited by PubMed Abstract: Legionella pneumophila is an opportunistic pathogen infecting alveolar macrophages and protozoa species. Legionella utilizes a Type IV Secretion System (T4SS) to translocate over 300 effector proteins into its host cell. In a recent study, we have isolated and solved the cryo-EM structure of the Type IV Coupling Complex (T4CC), a large cytoplasmic determinant associated with the inner membrane that recruits effector proteins for delivery to the T4SS for translocation. The T4CC is composed of a DotLMNYZ hetero-pentameric core from which the flexible IcmSW module flexibly protrudes. The DotY and DotZ proteins were newly reported members of this complex and their role remained elusive. In this study, we observed the effect of deleting DotY and DotZ on T4CC stability and localization. Furthermore, we found these two proteins are co-dependent, whereby the deletion of DotY resulted in DotZ absence from the coupling complex, and vice versa. Additional cryo-EM data analysis revealed the dynamic movement of the IcmSW module is modified by the DotY/Z proteins. We therefore determined the likely function of DotY and DotZ and revealed their importance on T4CC function. PubMed: 34816517DOI: 10.1111/mmi.14847 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.61 Å) |
Structure validation
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