2KEH

Plantaricin K in TFE

Summary for 2KEH

• Entry DOI: 10.2210/pdb2keh/pdb
• NMR Information: BMRB: 16149
• Descriptor: PlnK (1 entity in total)
• Functional Keywords: protein, antimicrobial protein
• Biological source: Lactobacillus plantarum
• Total number of polymer chains: 1
• Total formula weight: 3509.96

Authors

Rogne, P.,Haugen, M.,Nissen-Meyer, J.,Kristiansen, P. (deposition date: 2009-01-30, release date: 2009-07-07, Last modification date: 2024-05-22)

Primary citation

Rogne, P.,Haugen, C.,Fimland, G.,Nissen-Meyer, J.,Kristiansen, P.E.
Three-dimensional structure of the two-peptide bacteriocin plantaricin JK.
Peptides, 30:1613-1621, 2009

PubMed Abstract: The three-dimensional structures of the two peptides, PlnJ and PlnK, that constitutes the two-peptide bacteriocin plantaricin JK have been solved in water/TFE and water/DPC-micellar solutions using nuclear magnetic resonance (NMR) spectroscopy. PlnJ, a 25 residue peptide, has an N-terminal amphiphilic alpha-helix between Trp-3 and Tyr-15. The 32 residues long PlnK forms a central amphiphilic alpha-helix between Gly-9 and Leu-24. Measurements of the effect on anti-microbial activity of single glycine replacements in PlnJ and PlnK show that Gly-13 and Gly-17 in both peptides are very sensitive, giving more than a 100-fold reduction in activity when large residues replace glycine. In variants where other glycine residues, Gly-20 in PlnJ and Gly-7, Gly-9, Gly-24 and Gly-25 in PlnK, were replaced, the activity was reduced less than 10-fold. It is proposed that the detrimental effect on activity when exchanging Gly-13 and Gly-17 in PlnJ and PlnK is a result of reduced ability of the two peptides to interact through the GxxxG-motifs constituting Gly-13 and Gly-17.

PubMed: 19538999
DOI: 10.1016/j.peptides.2009.06.010

Experimental method

SOLUTION NMR