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

• Published in: Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2001-02, Vol.57 (2), p.317-319
• Main Authors: Abergel, Chantal, Walburger, Anne, Chenivesse, Sabine, Lazdunski, Claude
• Format: Article
• Language: English
• Subjects: Bacterial Outer Membrane Proteins; Crystallization; Crystallography, X-Ray; Escherichia coli; Escherichia coli - genetics; Escherichia coli - metabolism; Escherichia coli Proteins; Lipoproteins - chemistry; Lipoproteins - isolation & purification; Pal; Peptide Fragments - chemistry; peptidoglycan; Peptidoglycan - chemistry; Peptidoglycan - isolation & purification; Polymerase Chain Reaction; Proteoglycans; Recombinant Proteins - chemistry; Recombinant Proteins - isolation & purification; Tol-Pal system
• ISSN: 1399-0047; 0907-4449; 1399-0047
• DOI: 10.1107/S0907444900019739

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 I41, with unit‐cell parameters a = b = 89.3, c = 67.2 Å. There are two molecules in the asymmetric unit. Frozen crystals diffract to at least 2.8 Å resolution using synchrotron radiation. Selenomethionine‐substituted truncated Pal protein is currently being produced in order to use multiwavelength anomalous dispersion (MAD) for phasing.