9OIL
Solution Structure of the Broadspectrum Bacteriocin Garvicin Q
Summary for 9OIL
| Entry DOI | 10.2210/pdb9oil/pdb |
| NMR Information | BMRB: 53020 |
| Descriptor | Prepeptide GarQ (1 entity in total) |
| Functional Keywords | antibiotic, bacteriocin, lactic acid bacteria, alpha helix, mannose phospho-transferase system |
| Biological source | Lactococcus garvieae |
| Total number of polymer chains | 1 |
| Total formula weight | 5349.95 |
| Authors | Mallett, T.M.,Lamer, T.,Aleksandrzak-Piekarczyk, T.,Mckay, R.T.,Sit, C.S.,Rainey, J.K.,Van Belkum, M.,Vederas, J.C. (deposition date: 2025-05-06, release date: 2025-08-20, Last modification date: 2025-09-10) |
| Primary citation | Mallett, T.,Lamer, T.,Aleksandrzak-Piekarczyk, T.,McKay, R.T.,Catenza, K.,Sit, C.,Rainey, J.K.,Towle-Straub, K.M.,Vederas, J.C.,van Belkum, M.J. Solution Structure of the Broad-Spectrum Bacteriocin Garvicin Q. Int J Mol Sci, 26:-, 2025 Cited by PubMed Abstract: Class IId bacteriocins are linear, unmodified antimicrobial peptides produced by Gram-positive bacteria, and often display potent, narrow-spectrum inhibition spectra. Garvicin Q (GarQ) is a class IId bacteriocin produced by the lactic acid bacterium . It stands out for its unusual broad-spectrum antimicrobial activity against various bacterial species, including , , , , and spp. Its protein target is the mannose phosphotransferase system (Man-PTS) of susceptible bacterial strains, though little is known about the precise molecular mechanism behind GarQ's unusual broad spectrum of activity. In this work, C- and N-labelled GarQ was recombinantly produced using our previously described "sandwiched" protein expression system in . We also developed a protocol to purify a uniformly labelled sample of the small ubiquitin-like modifier His-SUMO, which is produced as a byproduct of the expression procedure. We demonstrated its use as a "free" protein standard for 3D NMR experiment calibrations. The GarQ solution structure was solved using triple-resonance nuclear magnetic resonance (NMR) spectroscopy and was compared with the structures of other Man-PTS-targeting bacteriocins. GarQ adopts a helix-hinge-helix fold, which is contrary to its structural predictions according to AlphaFold 3. PubMed: 40869166DOI: 10.3390/ijms26167846 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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