Crystallization and preliminary X-ray crystallographic analysis of the 38-kDa immunodominant antigen of Mycobacterium tuberculosis.
The 38-kDa lipoprotein is one of the most potent cell surface immunogens of Mycobacterium tuberculosis in antibody-and T cell-mediated reactions. Using a pure recombinant form of the protein, we have recently shown that it binds phosphate much like that of the phosphate-binding protein (M(r) = 34.4 kDa) that is localized in the periplasm of Escherichia coli and is involved as an initial receptor for active transport of phosphate. The purified 38-kDa protein has been crystallized in 2 forms that are suitable for high-resolution structural analyses. One form belongs to the monoclinic space group P2(1) with unit cell dimensions of a = 67.42 A, b = 113.38 A, c = 42.68 A, and beta = 108.53 degrees. The other is of orthorhombic space group P2(1)2(1)2 with a = 125.46 A, b = 72.27 A, and c = 73.43 A. Both crystal forms diffract to about 2 A resolution on a fine focus rotating anode.
Choudhary
A
A
Howard Hughes Medical Institute, Baylor College of Medicine, Houston, Texas 77030, USA.
Vyas
M N
MN
Vyas
N K
NK
Chang
Z
Z
Quiocho
F A
FA
D000942:Antigens, Bacterial / Q000737:chemistry* / Q000276:immunology; D003460:Crystallization; D018360:Crystallography, X-Ray; D016056:Immunodominant Epitopes / Q000737:chemistry / Q000276:immunology*; D008074:Lipoproteins / Q000737:chemistry* / Q000276:immunology; D009169:Mycobacterium tuberculosis / Q000737:chemistry / Q000276:immunology*
C075966:Ag38 antigen, Mycobacterium tuberculosis; D000942:Antigens, Bacterial; D016056:Immunodominant Epitopes; D008074:Lipoproteins