2K98

Helical hairpin structure of potent antimicrobial peptide MSI-594 in the presence of Lipopolysaccharide micelle

Summary for 2K98

Entry DOI	10.2210/pdb2k98/pdb
Descriptor	MSI-594 (1 entity in total)
Functional Keywords	msi-594, lps, trnoe, antimicrobial peptide, antimicrobial protein
Total number of polymer chains	1
Total formula weight	2447.10
Authors	Bhunia, A.,Bhattacharjya, S.,Ramamoorthy, A. (deposition date: 2008-09-30, release date: 2009-02-10, Last modification date: 2024-05-29)
Primary citation	Bhunia, A.,Ramamoorthy, A.,Bhattacharjya, S. Helical Hairpin Structure of a Potent Antimicrobial Peptide MSI-594 in Lipopolysaccharide Micelles by NMR Spectroscopy Chemistry, 15:2036-2040, 2009 Cited by PubMed Abstract: Essential understanding: Elucidation of structural requirements and interactions of antimicrobial peptides with lipopolysaccharide (LPS) are essential to understand the mechanism of action of antimicrobial peptides. The highly active antimicrobial peptide MSI-594 (see figure for electrostatic potential surface) acquires a novel helical hairpin structure in complex with LPS. The structure and interactions of MSI-594 with LPS presented here provide important insights into the mechanism of outer membrane permeabilization by antimicrobial peptides. PubMed: 19180607 DOI: 10.1002/chem.200802635 PDB entries with the same primary citation
Experimental method	SOLUTION NMR

Structure validation