Crystallization and preliminary crystallographic study of the outer-membrane lipoprotein receptor LolB, a member of the lipoprotein localization factors.
The Lol system mediates the translocation of the water-insoluble outer-membrane lipoprotein across the periplasm of Gram-negative bacteria depending on the sorting signal. The outer-membrane lipoprotein receptor LolB (21.2 kDa) is a member of the Lol system. A soluble mutant of LolB (mLolB) from Escherichia coli was crystallized in two forms. Monoclinic crystals diffract X-rays to 1.9 A resolution and belong to space group P2(1), with unit-cell parameters a = 37.2, b = 112.4, c = 47.8 A, beta = 111.4 degrees. The V(M) value is most likely to be 2.2 A(3) Da(-1), assuming the presence of two molecules in the asymmetric unit. Hexagonal crystals diffract X-rays to 2.2 A resolution and belong to space group P6(3)22, with unit-cell parameters a = b = 71.4, c = 133.9 A. The V(M) value is determined as 2.3 A(3) Da(-1), assuming a single molecule in the asymmetric unit. A four-wavelength data set was collected from a monoclinic crystal of selenomethionylated mLolB in order to perform MAD phasing. The quality of the initial electron-density map was sufficient to build a molecular model.
Takeda
Kazuki
K
RIKEN Harima Institute/SPring-8, Koto 1-1-1, Mikazuki-cho, Sayo-gun, Hyogo 679-5148, Japan.
Miyatake
Hideyuki
H
Yokota
Naoko
N
Matsuyama
Shin Ichi
SI
Tokuda
Hajime
H
Miki
Kunio
K
D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000235:genetics; D002352:Carrier Proteins / Q000737:chemistry* / Q000235:genetics; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics; D008958:Models, Molecular; D018832:Molecular Chaperones; D009154:Mutation; D012995:Solubility
D001425:Bacterial Outer Membrane Proteins; D002352:Carrier Proteins; D029968:Escherichia coli Proteins; C087012:LolB protein, E coli; D018832:Molecular Chaperones