2MIJ
NMR structure of the S-linked glycopeptide sublancin 168
Summary for 2MIJ
| Entry DOI | 10.2210/pdb2mij/pdb |
| NMR Information | BMRB: 19683 |
| Descriptor | SPBc2 prophage-derived bacteriocin sublancin-168, beta-D-glucopyranose (2 entities in total) |
| Functional Keywords | glycopeptide, antimicrobial protein |
| Biological source | Bacillus subtilis |
| Cellular location | Secreted: P68577 |
| Total number of polymer chains | 1 |
| Total formula weight | 3903.45 |
| Authors | Garcia De Gonzalo, C.V.,Zhu, L.,Oman, T.J.,van der Donk, W.A. (deposition date: 2013-12-13, release date: 2014-03-12, Last modification date: 2024-11-20) |
| Primary citation | Garcia De Gonzalo, C.V.,Zhu, L.,Oman, T.J.,van der Donk, W.A. NMR structure of the s-linked glycopeptide sublancin 168. Acs Chem.Biol., 9:796-801, 2014 Cited by PubMed Abstract: Sublancin 168 is a member of a small group of glycosylated antimicrobial peptides known as glycocins. The solution structure of sublancin 168, a 37-amino-acid peptide produced by Bacillus subtilis 168, has been solved by nuclear magnetic resonance (NMR) spectroscopy. Sublancin comprises two α-helices and a well-defined interhelical loop. The two helices span residues 6-16 and 26-35, and the loop region encompasses residues 17-25. The 9-amino-acid loop region contains a β-S-linked glucose moiety attached to Cys22. Hydrophobic interactions as well as hydrogen bonding are responsible for the well-structured loop region. The three-dimensional structure provides an explanation for the previously reported extraordinary high stability of sublancin 168. PubMed: 24405370DOI: 10.1021/cb4008106 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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