6O8R
Syn-safencin 24
Summary for 6O8R
| Entry DOI | 10.2210/pdb6o8r/pdb |
| NMR Information | BMRB: 30587 |
| Descriptor | Circular bacteriocin, circularin A/uberolysin family (1 entity in total) |
| Functional Keywords | antimicrobial, synthetic peptide, antimicrobial protein |
| Biological source | Bacillus safensis |
| Total number of polymer chains | 1 |
| Total formula weight | 3061.82 |
| Authors | Fields, F.R.,Lee, S.W. (deposition date: 2019-03-11, release date: 2020-05-13, Last modification date: 2024-05-15) |
| Primary citation | Fields, F.R.,Manzo, G.,Hind, C.K.,Janardhanan, J.,Foik, I.P.,Carmo Silva, P.D.,Balsara, R.D.,Clifford, M.,Vu, H.M.,Ross, J.N.,Kalwajtys, V.R.,Gonzalez, A.J.,Bui, T.T.,Ploplis, V.A.,Castellino, F.J.,Siryaporn, A.,Chang, M.,Sutton, J.M.,Mason, A.J.,Lee, S. Synthetic Antimicrobial Peptide Tuning Permits Membrane Disruption and Interpeptide Synergy. Acs Pharmacol Transl Sci, 3:418-424, 2020 Cited by PubMed Abstract: The ribosomally produced antimicrobial peptides of bacteria (bacteriocins) represent an unexplored source of membrane-active antibiotics. We designed a library of linear peptides from a circular bacteriocin and show that pore-formation dynamics in bacterial membranes are tunable via selective amino acid substitution. We observed antibacterial interpeptide synergy indicating that fundamentally altering interactions with the membrane enables synergy. Our findings suggest an approach for engineering pore-formation through rational peptide design and increasing the utility of novel antimicrobial peptides by exploiting synergy. PubMed: 32566907DOI: 10.1021/acsptsci.0c00001 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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