7NEF
Fucosylated linear peptide Fln65 bound to the fucose binding lectin LecB PA-IIL from Pseudomonas aeruginosa at 1.5 Angstrom resolution
Summary for 7NEF
| Entry DOI | 10.2210/pdb7nef/pdb |
| Descriptor | Fucose-binding lectin, Fln65, CALCIUM ION, ... (5 entities in total) |
| Functional Keywords | antimicrobial peptide, lectin, antibiotic |
| Biological source | Pseudomonas aeruginosa More |
| Total number of polymer chains | 16 |
| Total formula weight | 107816.81 |
| Authors | Personne, H.,Baeriswyl, S.,Stocker, A.,Reymond, J.-L. (deposition date: 2021-02-03, release date: 2021-03-03, Last modification date: 2024-10-23) |
| Primary citation | Baeriswyl, S.,Personne, H.,Di Bonaventura, I.,Kohler, T.,van Delden, C.,Stocker, A.,Javor, S.,Reymond, J.L. A mixed chirality alpha-helix in a stapled bicyclic and a linear antimicrobial peptide revealed by X-ray crystallography. Rsc Chem Biol, 2:1608-1617, 2021 Cited by PubMed Abstract: The peptide α-helix is right-handed when containing amino acids with l-chirality, and left-handed with d-chirality, however mixed chirality peptides generally do not form α-helices unless a helix inducer such as the non-natural residue amino-isobutyric acid is used. Herein we report the first X-ray crystal structures of mixed chirality α-helices in short peptides comprising only natural residues as the example of a stapled bicyclic and a linear membrane disruptive amphiphilic antimicrobial peptide (AMP) containing seven l- and four d-residues, as complexes of fucosylated analogs with the bacterial lectin LecB. The mixed chirality α-helices are superimposable onto the homochiral α-helices and form under similar conditions as shown by CD spectra and MD simulations but non-hemolytic and resistant to proteolysis. The observation of a mixed chirality α-helix with only natural residues in the protein environment of LecB suggests a vast unexplored territory of α-helical mixed chirality sequences and their possible use for optimizing bioactive α-helical peptides. PubMed: 34977576DOI: 10.1039/d1cb00124h PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.51 Å) |
Structure validation
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