Crystal structure and functional implications of LprF fromMycobacterium tuberculosisandM. bovis
The Gram-positive bacteriaMycobacterium tuberculosisandM. bovisare causative agents of tuberculosis in humans and cattle. The lipoprotein LprF is found inM. tuberculosisandM. bovisbut not in the nonpathogenicM. smegmatis. To date, the role of LprF remains to be elucidated. In this study, the crystal structure of LprF has been determined at 1.1 Å resolution. The overall structure is similar to that of a homologue, LprG, with a central hydrophobic cavity that binds a triacylated glycolipid. LprF exhibited a central cavity structure similar to that of LprG, but with a smaller cavity that binds two alkyl chains. Consistently, subsequent mass-spectrometric analysis revealed that the bound ligand was a diacylated glycolipid, as found in the structure. Furthermore, an increased ratio of lipoarabinomannan to lipomannan in the mycobacterial cell wall was observed whenlprFwas introduced intoM. smegmatis. These observations suggested that LprF transfers the diacylated glycolipid from the plasma membrane to the cell wall, which might be related to the pathogenesis of the bacteria.