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

被引:19
作者
Abergel, C
Walburger, A
Chenivesse, S
Lazdunski, C
机构
[1] AVENTIS, CNRS, UMR 1899, F-13402 Marseille 20, France
[2] Lab Ingn Syst Macromol, UPR 9027, F-13402 Marseille, France
来源
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 2001年 / 57卷
关键词
D O I
10.1107/S0907444900019739
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
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 Gramnegative 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 Angstrom. There are two molecules in the asymmetric unit. Frozen crystals diffract to at least 2.8 Angstrom resolution using synchrotron radiation. Selenomethionine-substituted truncated Pal protein is currently being produced in order to use multiwavelength anomalous dispersion (MAD) for phasing.
引用
收藏
页码:317 / 319
页数:3
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