PMID:11173492
| Citation |
Abergel, C, Walburger, A, Chenivesse, S and Lazdunski, C (2001) Crystallization and preliminary crystallographic study of the peptidoglycan-associated lipoprotein from Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 57:317-9 |
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| 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. |
| Links | |
| Keywords |
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 |
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