PMID:10843861
| Citation |
Shu, W, Liu, J, Ji, H and Lu, M (2000) Core structure of the outer membrane lipoprotein from Escherichia coli at 1.9 A resolution. J. Mol. Biol. 299:1101-12 |
|---|---|
| Abstract |
The outer membrane lipoprotein of the Escherichia coli cell envelope has characteristic lipid modifications at an amino-terminal cysteine and can exist in a form bound covalently to the peptidoglycan through a carboxyl-terminal lysine. The 56-residue polypeptide moiety of the lipoprotein, designated Lpp-56, folds into a stable, trimeric helical structure in aqueous solution. The 1.9 A resolution crystal structure of Lpp-56 comprises a parallel three-stranded coiled coil including a novel alanine-zipper unit and two helix-capping motifs. The amino-terminal motif forms a hydrogen-bonding network anchoring an umbrella-shaped fold. The carboxyl-terminal motif uses puckering of the tyrosine side-chains as a unique docking arrangement in helix termination. The structure provides an explanation for assembly and insertion of the lipoprotein molecules into the outer membrane of gram-negative bacteria and suggests a molecular target for antibacterial drug discovery. |
| Links |
PubMed Online version:10.1006/jmbi.2000.3776 |
| Keywords |
Alanine/chemistry; Alanine/metabolism; Amino Acid Motifs; Amino Acid Sequence; Bacterial Outer Membrane Proteins/chemistry; Bacterial Outer Membrane Proteins/metabolism; Carrier Proteins/chemistry; Carrier Proteins/metabolism; Circular Dichroism; Crystallography, X-Ray; Escherichia coli/chemistry; Escherichia coli Proteins; Hydrogen Bonding; Lipoproteins; Models, Molecular; Molecular Sequence Data; Peptide Fragments/chemistry; Peptide Fragments/metabolism; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; Recombinant Proteins/chemistry; Recombinant Proteins/metabolism; Sequence Alignment; Structure-Activity Relationship; Thermodynamics |
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