2KV5
Solution structure of the par toxin Fst in DPC micelles
Summary for 2KV5
| Entry DOI | 10.2210/pdb2kv5/pdb |
| Descriptor | Putative uncharacterized protein RNAI (1 entity in total) |
| Functional Keywords | toxin-antitoxin, bacterial, toxin |
| Biological source | Enterococcus faecalis |
| Total number of polymer chains | 1 |
| Total formula weight | 3767.48 |
| Authors | Zangger, K.,Gobl, C.,Kosol, S.,Ruckert, H.M. (deposition date: 2010-03-08, release date: 2011-02-02, Last modification date: 2024-05-01) |
| Primary citation | Gobl, C.,Kosol, S.,Stockner, T.,Ruckert, H.M.,Zangger, K. Solution structure and membrane binding of the toxin fst of the par addiction module Biochemistry, 49:6567-6575, 2010 Cited by PubMed Abstract: The par toxin-antitoxin system is required for the stable inheritance of the plasmid pAD1 in its native host Enterococcus faecalis. It codes for the toxin Fst and a small antisense RNA which inhibits translation of toxin mRNA, and it is the only known antisense regulated toxin-antitoxin system in Gram-positive bacteria. This study presents the structure of the par toxin Fst, the first atomic resolution structure of a component of an antisense regulated toxin-antitoxin system. The mode of membrane binding was determined by relaxation enhancements in a paramagnetic environment and molecular dynamics simulation. Fst forms a membrane-binding alpha-helix in the N-terminal part and contains an intrinsically disordered region near the C-terminus. It binds in a transmembrane orientation with the C-terminus likely pointing toward the cytosol. Membrane-bound, alpha-helical peptides are frequently found in higher organisms as components of the innate immune system. Despite similarities to these antimicrobial peptides, Fst shows neither hemolytic nor antimicrobial activity when applied externally to a series of bacteria, fungal cells, and erythrocytes. Moreover, its charge distribution, orientation in the membrane, and structure distinguish it from antimicrobial peptides. PubMed: 20677831DOI: 10.1021/bi1005128 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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