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| Title | The three-dimensional structure of carnocyclin A reveals that many circular bacteriocins share a common structural motif. |
|---|---|
| Journal, issue, pages | J. Biol. Chem., Vol. 284, Page 28674-28681, Year 2009 |
| Publish date | May 28, 2009 (structure data deposition date) |
Authors | Martin-Visscher, L.A. / Gong, X. / Duszyk, M. / Vederas, J.C. |
External links | J. Biol. Chem. / PubMed:19692336 |
| Methods | NMR (solution) |
| Structure data | ![]() PDB-2kjf: |
| Source |
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Keywords | ANTIMICROBIAL PROTEIN / circular bacteriocin / antimicrobial peptide / helical / saposin-fold / Antibiotic / Antimicrobial / Bacteriocin |
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carnobacterium maltaromaticum (bacteria)
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