5UJR
NMR Solution Structure of the Two-component Bacteriocin CbnXY
Summary for 5UJR
| Entry DOI | 10.2210/pdb5ujr/pdb |
| NMR Information | BMRB: 30236 |
| Descriptor | Bacteriocin (1 entity in total) |
| Functional Keywords | antimicrobial protein |
| Biological source | Carnobacterium maltaromaticum |
| Total number of polymer chains | 1 |
| Total formula weight | 3590.18 |
| Authors | Acedo, J.Z.,Towle, K.M.,Lohans, C.T.,McKay, R.T.,Miskolzie, M.,Doerksen, T.,Vederas, J.C.,Martin-Visscher, L.A. (deposition date: 2017-01-18, release date: 2017-11-29, Last modification date: 2024-05-15) |
| Primary citation | Acedo, J.Z.,Towle, K.M.,Lohans, C.T.,Miskolzie, M.,McKay, R.T.,Doerksen, T.A.,Vederas, J.C.,Martin-Visscher, L.A. Identification and three-dimensional structure of carnobacteriocin XY, a class IIb bacteriocin produced by Carnobacteria. FEBS Lett., 591:1349-1359, 2017 Cited by PubMed Abstract: In this study, we report that CbnX (33 residues) and CbnY (29 residues) comprise a class IIb (two-component) bacteriocin in Carnobacteria. Individually, CbnX and CbnY are inactive, but together act synergistically to exert a narrow spectrum of activity. The structures of CbnX and CbnY in structure-inducing conditions were determined and strongly resemble other class IIb bacteriocins (i.e., LcnG, PlnEF, PlnJK). CbnX has an extended, amphipathic α-helix and a flexible C terminus. CbnY has two α-helices (one hydrophobic, one amphipathic) connected by a short loop and a cationic C terminus. CbnX and CbnY do not appear to interact directly and likely require a membrane-bound receptor to facilitate formation of the bacteriocin complex. This is the first class IIb bacteriocin reported for Carnobacteria. PubMed: 28391617DOI: 10.1002/1873-3468.12648 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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