Crystallization and preliminary X-ray analysis of a C-terminal fragment of FlgJ, a putative flagellar rod cap protein from Salmonella.
The formation of the bacterial flagellar axial structure, including the filament, the hook and the rod, requires the attachment of a cap complex to the distal end of the growing structure. Because the rod penetrates the peptidoglycan (PG) layer, the rod cap complex is thought to have PG-hydrolyzing activity. FlgJ is a putative rod cap protein whose C-terminal region shows sequence similarity to known muramidases. In this study, FlgJ(120-316), a C-terminal fragment of FlgJ which contains the muramidase region, was overproduced, purified and crystallized. Crystals were obtained by the sitting-drop vapour-diffusion technique using PEG 3350 as a crystallizing agent and belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 38.8, b = 43.9, c = 108.5 A. Anomalous difference Patterson maps calculated from the diffraction data set of a selenomethionine-labelled crystal showed significant peaks in the Harker sections, indicating that the data were suitable for structure determination.
Kikuchi
Yuki
Y
Graduate School of Frontier Biosciences, Osaka University, Japan.
Matsunami
Hideyuki
H
Yamane
Midori
M
Imada
Katsumi
K
Namba
Keiichi
K
D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D005407:Flagella / Q000378:metabolism; D006868:Hydrolysis; D008968:Molecular Conformation; D015394:Molecular Structure; D009113:Muramidase / Q000737:chemistry* / Q000502:physiology; D010457:Peptidoglycan / Q000737:chemistry; D011092:Polyethylene Glycols / Q000737:chemistry; D017434:Protein Structure, Tertiary; D012475:Salmonella / Q000378:metabolism*; D014508:Urea / Q000737:chemistry; D014965:X-Rays
D001426:Bacterial Proteins; D010457:Peptidoglycan; D011092:Polyethylene Glycols; D014508:Urea; D009113:Muramidase