9EZM
CryoEM structure of the contracted sheath in H. borinquense
Summary for 9EZM
| Entry DOI | 10.2210/pdb9ezm/pdb |
| EMDB information | 50089 |
| Descriptor | Phage tail sheath protein FI (1 entity in total) |
| Functional Keywords | archaea, contractile injection system, sheath, cryoem, structural protein |
| Biological source | Halogeometricum borinquense DSM 11551 |
| Total number of polymer chains | 18 |
| Total formula weight | 1139774.76 |
| Authors | Zachs, T.,Malit, J.J.,Xu, J.,Schuerch, A.,Sivabalasarma, S.,Nussbaum, P.,Albers, S.V.,Pilhofer, M. (deposition date: 2024-04-12, release date: 2024-11-27) |
| Primary citation | Zachs, T.,Malit, J.J.L.,Xu, J.,Schurch, A.,Sivabalasarma, S.,Nussbaum, P.,Albers, S.V.,Pilhofer, M. Archaeal type six secretion system mediates contact-dependent antagonism. Sci Adv, 10:eadp7088-eadp7088, 2024 Cited by PubMed Abstract: Microbial communities are shaped by cell-cell interactions. Although archaea are often found in associations with other microorganisms, the mechanisms structuring these communities are poorly understood. Here, we report on the structure and function of haloarchaeal contractile injection systems (CISs). Using a combination of functional assays and time-lapse imaging, we show that exhibits antagonism toward by inducing cell lysis and inhibiting proliferation. This antagonism is contact-dependent and requires a functional CIS, which is encoded by a gene cluster that is associated with toxin-immunity pairs. Cryo-focused ion beam milling and imaging by cryo-electron tomography revealed that these CISs are bound to the cytoplasmic membrane, resembling the bacterial type six secretion systems (T6SSs). We show that related T6SS gene clusters are conserved and expressed in other haloarchaeal strains, which exhibit antagonistic behavior. Our data provide a mechanistic framework for understanding how archaea may shape microbial communities and affect the food webs they inhabit. PubMed: 39546591DOI: 10.1126/sciadv.adp7088 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.9 Å) |
Structure validation
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