2MP8
NMR structure of NKR-5-3B
Summary for 2MP8
| Entry DOI | 10.2210/pdb2mp8/pdb |
| NMR Information | BMRB: 19970 |
| Descriptor | NKR-5-3B (1 entity in total) |
| Functional Keywords | bacteriocin, antimicrobial peptide, head-to-tail cyclic, helix bundle, antimicrobial protein |
| Biological source | Enterococcus faecalis |
| Total number of polymer chains | 1 |
| Total formula weight | 6340.49 |
| Authors | Rosengren, K.J.,Craik, D.J. (deposition date: 2014-05-13, release date: 2015-05-13, Last modification date: 2024-10-09) |
| Primary citation | Himeno, K.,Rosengren, K.J.,Inoue, T.,Perez, R.H.,Colgrave, M.L.,Lee, H.S.,Chan, L.Y.,Henriques, S.T.,Fujita, K.,Ishibashi, N.,Zendo, T.,Wilaipun, P.,Nakayama, J.,Leelawatcharamas, V.,Jikuya, H.,Craik, D.J.,Sonomoto, K. Identification, Characterization, and Three-Dimensional Structure of the Novel Circular Bacteriocin, Enterocin NKR-5-3B, from Enterococcus faecium Biochemistry, 54:4863-4876, 2015 Cited by PubMed Abstract: Enterocin NKR-5-3B, one of the multiple bacteriocins produced by Enterococcus faecium NKR-5-3, is a 64-amino acid novel circular bacteriocin that displays broad-spectrum antimicrobial activity. Here we report the identification, characterization, and three-dimensional nuclear magnetic resonance solution structure determination of enterocin NKR-5-3B. Enterocin NKR-5-3B is characterized by four helical segments that enclose a compact hydrophobic core, which together with its circular backbone impart high stability and structural integrity. We also report the corresponding structural gene, enkB, that encodes an 87-amino acid precursor peptide that undergoes a yet to be described enzymatic processing that involves adjacent cleavage and ligation of Leu(24) and Trp(87) to yield the mature (circular) enterocin NKR-5-3B. PubMed: 26174911DOI: 10.1021/acs.biochem.5b00196 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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