4QA8
Crystal structure of LprF from Mycobacterium bovis
Summary for 4QA8
Entry DOI | 10.2210/pdb4qa8/pdb |
Descriptor | Putative lipoprotein LprF, (2R)-2-(dodecanoyloxy)propyl (4E,6E,8E,10E,12E)-pentadeca-4,6,8,10,12-pentaenoate (3 entities in total) |
Functional Keywords | lipid transfer, diacylated glycolipid, lipid transport |
Biological source | Mycobacterium bovis |
Cellular location | Cell membrane ; Lipid-anchor : P65315 |
Total number of polymer chains | 1 |
Total formula weight | 24200.45 |
Authors | |
Primary citation | Kim, J.S.,Jiao, L.,Oh, J.I.,Ha, N.C.,Kim, Y.H. Crystal structure and functional implications of LprF from Mycobacterium tuberculosis and M. bovis Acta Crystallogr.,Sect.D, 70:2619-2630, 2014 Cited by PubMed Abstract: The Gram-positive bacteria Mycobacterium tuberculosis and M. bovis are causative agents of tuberculosis in humans and cattle. The lipoprotein LprF is found in M. tuberculosis and M. bovis but not in the nonpathogenic M. 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 when lprF was introduced into M. 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. PubMed: 25286846DOI: 10.1107/S1399004714016599 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.1 Å) |
Structure validation
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