1VM3
Solution structure of a membrane-targeting peptide designed based on the N-terminal sequence of E. coli enzyme IIA (Glucose)
Summary for 1VM3
| Entry DOI | 10.2210/pdb1vm3/pdb |
| Related | 1O53 1vm2 1vm4 1vm5 |
| Descriptor | peptide A3 (1 entity in total) |
| Functional Keywords | amphipathic helix, antimicrobial peptide, bacterial membrane anchor, membrane binding, antibiotic |
| Biological source | synthetic construct |
| Total number of polymer chains | 1 |
| Total formula weight | 1438.67 |
| Authors | |
| Primary citation | Wang, G.,Li, Y.,Li, X. Correlation of Three-dimensional Structures with the Antibacterial Activity of a Group of Peptides Designed Based on a Nontoxic Bacterial Membrane Anchor. J.Biol.Chem., 280:5803-5811, 2005 Cited by PubMed Abstract: To understand the functional differences between a nontoxic membrane anchor corresponding to the N-terminal sequence of the Escherichia coli enzyme IIA(Glc) and a toxic antimicrobial peptide aurein 1.2 of similar sequence, a series of peptides was designed to bridge the gap between them. An alteration of a single residue of the membrane anchor converted it into an antibacterial peptide. Circular dichroism spectra indicate that all peptides are disordered in water but helical in micelles. Structures of the peptides were determined in membrane-mimetic micelles by solution NMR spectroscopy. The quality of the distance-based structures was improved by including backbone angle restraints derived from a set of chemical shifts ((1)H(alpha), (15)N, (13)C(alpha), and (13)C(beta)) from natural abundance two-dimensional heteronuclear correlated spectroscopy. Different from the membrane anchor, antibacterial peptides possess a broader and longer hydrophobic surface, allowing a deeper penetration into the membrane, as supported by intermolecular nuclear Overhauser effect cross-peaks between the peptide and short chain dioctanoyl phosphatidylglycerol. An attempt was made to correlate the NMR structures of these peptides with their antibacterial activity. The activity of this group of peptides does not correlate exactly with helicity, amphipathicity, charge, the number of charges, the size of the hydrophobic surface, or hydrophobic transfer free energy. However, a correlation is established between the peptide activity and membrane perturbation potential, which is defined by interfacial hydrophobic patches and basic residues in the case of cationic peptides. Indeed, (31)P solid state NMR spectroscopy of lipid bilayers showed that the extent of lipid vesicle disruption by these peptides is proportional to their membrane perturbation potential. PubMed: 15572363DOI: 10.1074/jbc.M410116200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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