4AX2
New Type VI-secreted toxins and self-resistance proteins in Serratia marcescens
Summary for 4AX2
| Entry DOI | 10.2210/pdb4ax2/pdb |
| Descriptor | RAP1B, IODIDE ION, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | toxin, resistance protein, helical fold, s-sad phasing |
| Biological source | SERRATIA MARCESCENS |
| Total number of polymer chains | 1 |
| Total formula weight | 16928.50 |
| Authors | English, G.,Trunk, K.,Rao, V.A.,Srikannathasan, V.,Fritsch, M.J.,Guo, M.,Hunter, W.N.,Coulthurst, S.J. (deposition date: 2012-06-07, release date: 2012-09-19, Last modification date: 2013-07-17) |
| Primary citation | English, G.,Trunk, K.,Rao, V.A.,Srikannathasan, V.,Hunter, W.N.,Coulthurst, S.J. New Secreted Toxins and Immunity Proteins Encoded within the Type Vi Secretion System Gene Cluster of Serratia Marcescens Mol.Microbiol., 86:921-, 2012 Cited by PubMed Abstract: Protein secretion systems are critical to bacterial virulence and interactions with other organisms. The Type VI secretion system (T6SS) is found in many bacterial species and is used to target either eukaryotic cells or competitor bacteria. However, T6SS-secreted proteins have proven surprisingly elusive. Here, we identified two secreted substrates of the antibacterial T6SS from the opportunistic human pathogen, Serratia marcescens. Ssp1 and Ssp2, both encoded within the T6SS gene cluster, were confirmed as antibacterial toxins delivered by the T6SS. Four related proteins encoded around the Ssp proteins ('Rap' proteins) included two specifically conferring self-resistance ('immunity') against T6SS-dependent Ssp1 or Ssp2 toxicity. Biochemical characterization revealed specific, tight binding between cognate Ssp-Rap pairs, forming complexes of 2:2 stoichiometry. The atomic structures of two Rap proteins were solved, revealing a novel helical fold, dependent on a structural disulphide bond, a structural feature consistent with their functional localization. Homologues of the Serratia Ssp and Rap proteins are found encoded together within other T6SS gene clusters, thus they represent founder members of new families of T6SS-secreted and cognate immunity proteins. We suggest that Ssp proteins are the original substrates of the S. marcescens T6SS, before horizontal acquisition of other T6SS-secreted toxins. Molecular insight has been provided into how pathogens utilize antibacterial T6SSs to overcome competitors and succeed in polymicrobial niches. PubMed: 22957938DOI: 10.1111/MMI.12028 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.88 Å) |
Structure validation
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