2KNS
Helical Hairpin Structure of Pardaxin in Lipopolysaccharide Micelles: Studied by NMR Spectroscopy
Summary for 2KNS
Entry DOI | 10.2210/pdb2kns/pdb |
Descriptor | Pardaxin P-4 (1 entity in total) |
Functional Keywords | pardaxin, pa4, lps, trnoe, antimicrobial peptide, std nmr, ion transport, porin, secreted, toxin, transmembrane, transport, antimicrobial protein |
Biological source | Pardachirus marmoratus (Red sea moses sole) |
Cellular location | Secreted: P81861 |
Total number of polymer chains | 1 |
Total formula weight | 3325.85 |
Authors | Bhunia, A.,Bhattacharjya, S.,Ramamoorthy, A. (deposition date: 2009-09-03, release date: 2009-12-15, Last modification date: 2024-05-29) |
Primary citation | Bhunia, A.,Domadia, P.N.,Torres, J.,Hallock, K.J.,Ramamoorthy, A.,Bhattacharjya, S. NMR structure of pardaxin, a pore-forming antimicrobial peptide, in lipopolysaccharide Micelles: Mechanism of outer membrane permeabilization J.Biol.Chem., 285:3883-3895, 2010 Cited by PubMed: 19959835DOI: 10.1074/jbc.M109.065672 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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