Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 299, Issue 4, Pages 1101-1112Publisher
ACADEMIC PRESS LTD
DOI: 10.1006/jmbi.2000.3776
Keywords
lipoprotein; outer membrane; protein folding; coiled coil; helix capping
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Funding
- NIAID NIH HHS [AI 42382] Funding Source: Medline
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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 Angstrom 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. (C) 2000 Academic Press.
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