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9EZM

CryoEM structure of the contracted sheath in H. borinquense

Summary for 9EZM
Entry DOI10.2210/pdb9ezm/pdb
EMDB information50089
DescriptorPhage tail sheath protein FI (1 entity in total)
Functional Keywordsarchaea, contractile injection system, sheath, cryoem, structural protein
Biological sourceHalogeometricum borinquense DSM 11551
Total number of polymer chains18
Total formula weight1139774.76
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 citationZachs, 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: 39546591
DOI: 10.1126/sciadv.adp7088
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.9 Å)
Structure validation

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