Crystallization and preliminary crystallographic study of the peptidoglycan-associated lipoprotein from Escherichia coli

Acta Crystallogr D Biol Crystallogr. 2001 Feb;57(Pt 2):317-9. doi: 10.1107/s0907444900019739.

Abstract

The peptidoglycan-associated lipoprotein (Pal) from Escherichia coli is part of the Tol--Pal multiprotein complex used by group A colicins to penetrate and kill cells. Pal homologues are found in many Gram-negative bacteria and the Tol--Pal system is thought to play a role in bacterial envelope integrity. The Pal protein comprises 152 amino acids. Crystals of the C-terminal 109-amino-acid fragment of the Pal protein have been produced. The crystals belong to the tetragonal space group I4(1), with unit-cell parameters a = b = 89.3, c = 67.2 A. There are two molecules in the asymmetric unit. Frozen crystals diffract to at least 2.8 A resolution using synchrotron radiation. Selenomethionine-substituted truncated Pal protein is currently being produced in order to use multiwavelength anomalous dispersion (MAD) for phasing.

MeSH terms

  • Bacterial Outer Membrane Proteins*
  • Crystallization
  • Crystallography, X-Ray
  • Escherichia coli / genetics
  • Escherichia coli / metabolism*
  • Escherichia coli Proteins
  • Lipoproteins / chemistry*
  • Lipoproteins / isolation & purification
  • Peptide Fragments / chemistry
  • Peptidoglycan / chemistry*
  • Peptidoglycan / isolation & purification
  • Polymerase Chain Reaction
  • Proteoglycans*
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification

Substances

  • Bacterial Outer Membrane Proteins
  • Escherichia coli Proteins
  • ExcC protein, E coli
  • Lipoproteins
  • Peptide Fragments
  • Peptidoglycan
  • Proteoglycans
  • Recombinant Proteins
  • PplA protein, Legionella pneumophila