Crystallization and preliminary crystallographic study of the peptidoglycan-associated lipoprotein from Escherichia coli.
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.
Abergel
C
C
Information Génétique et Structurale, UMR1889 CNRS-AVENTIS, 31 Chemin Joseph Aiguier, 13402 Marseille CEDEX 20, France. chantal@igs.cnrs-mrs.fr
Walburger
A
A
Chenivesse
S
S
Lazdunski
C
C
D001425:Bacterial Outer Membrane Proteins; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D029968:Escherichia coli Proteins; D008074:Lipoproteins / Q000737:chemistry* / Q000302:isolation & purification; D010446:Peptide Fragments / Q000737:chemistry; D010457:Peptidoglycan / Q000737:chemistry* / Q000302:isolation & purification; D016133:Polymerase Chain Reaction; D011509:Proteoglycans; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification
D001425:Bacterial Outer Membrane Proteins; D029968:Escherichia coli Proteins; C031163:ExcC protein, E coli; D008074:Lipoproteins; D010446:Peptide Fragments; D010457:Peptidoglycan; D011509:Proteoglycans; D011994:Recombinant Proteins; C069988:PplA protein, Legionella pneumophila