5LFI
lactococcin A immunity protein
Summary for 5LFI
| Entry DOI | 10.2210/pdb5lfi/pdb |
| NMR Information | BMRB: 34018 |
| Descriptor | Lactococcin-A immunity protein (1 entity in total) |
| Functional Keywords | four-helix bundle, immunity protein, bacteriocin receptor, immune system |
| Biological source | Lactococcus lactis subsp. lactis |
| Total number of polymer chains | 1 |
| Total formula weight | 13273.20 |
| Authors | Persson, C.,Fuochi, V.,Pedersen, A.,Karlsson, B.G.,Nissen-Meyer, J.,Kristiansen, P.E.,Oppegard, C. (deposition date: 2016-07-01, release date: 2016-11-16, Last modification date: 2024-06-19) |
| Primary citation | Kristiansen, P.E.,Persson, C.,Fuochi, V.,Pedersen, A.,Karlsson, G.B.,Nissen-Meyer, J.,Oppegard, C. Nuclear Magnetic Resonance Structure and Mutational Analysis of the Lactococcin A Immunity Protein. Biochemistry, 55:6250-6257, 2016 Cited by PubMed Abstract: The class IId bacteriocin lactococcin A and the pediocin-like bacteriocins induce membrane leakage and cell death by specifically binding the mannose phophotransferase system (man-PTS) on their target cells. The bacteriocins' cognate immunity proteins that protect the producer cell from its own bacteriocin recognize and bind to the bacteriocin-man-PTS complex and thereby block membrane leakage. In this study, we have determined the three-dimensional structure of the lactococcin A immunity protein (LciA) by the use of nuclear magnetic resonance spectroscopy. LciA forms a four-helix bundle structure with a flexible C-terminal tail. Despite the low degree of sequence similarity between LciA and the pediocin-like immunity proteins, they share the same fold. However, there are certain differences between the structures. The C-terminal helix in LciA is considerably shorter than that observed in the pediocin-like immunity proteins, and the surface potentials of the immunity proteins differ. Truncated variants of LciA in which 6 or 10 of the C-terminal residues were removed yielded a reduced degree of protection, indicating that the unstructured C-terminal tail is important for the functionality of the immunity proteins. PubMed: 27808503DOI: 10.1021/acs.biochem.6b00848 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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