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J Mol Biol. 2000 Jun 16;299(4):1101-12.

Core structure of the outer membrane lipoprotein from Escherichia coli at 1.9 A resolution.

Author information

  • 1Department of Biochemistry, Weill Medical College of Cornell University, New York, NY, 10021, USA.

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.

Copyright 2000 Academic Press.

PMID:
10843861
[PubMed - indexed for MEDLINE]
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