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

Wei Shu, Jie Liu, Hong Ji, Min Lu

Research output: Contribution to journalArticlepeer-review

79 Scopus citations

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 Å resolution crystal structure of Lpp-56 comprises a parallel three-stranded coiled coil including a novel alaninezipper 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.

Original languageEnglish (US)
Pages (from-to)1101-1112
Number of pages12
JournalJournal of molecular biology
Volume299
Issue number4
DOIs
StatePublished - Jun 16 2000

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology

Keywords

  • Coiled coil
  • Helix capping
  • Lipoprotein
  • Outer membrane
  • Protein folding

Fingerprint Dive into the research topics of 'Core structure of the outer membrane lipoprotein from Escherichia coli at 1.9 Å resolution'. Together they form a unique fingerprint.

Cite this