2BYO
Crystal structure of Mycobacterium tuberculosis lipoprotein LppX (Rv2945c)
Summary for 2BYO
| Entry DOI | 10.2210/pdb2byo/pdb |
| Descriptor | LIPOPROTEIN LPPX, ZINC ION, ACETATE ION, ... (8 entities in total) |
| Functional Keywords | lipoprotein, lipid transport, palmitate |
| Biological source | MYCOBACTERIUM TUBERCULOSIS |
| Cellular location | Cell membrane; Lipid-anchor (Potential): P65306 |
| Total number of polymer chains | 1 |
| Total formula weight | 23133.99 |
| Authors | Sulzenbacher, G.,Canaan, S.,Roig-Zamboni, V.,Maurin, D.,Gicquel, B.,Bourne, Y. (deposition date: 2005-08-03, release date: 2006-03-22, Last modification date: 2024-05-08) |
| Primary citation | Sulzenbacher, G.,Canaan, S.,Bordat, Y.,Neyrolles, O.,Stadthagen, G.,Roig-Zamboni, V.,Rauzier, J.,Maurin, D.,Laval, F.,Daffe, M.,Cambillau, C.,Gicquel, B.,Bourne, Y.,Jackson, M. Lppx is a Lipoprotein Required for the Translocation of Phthiocerol Dimycocerosates to the Surface of Mycobacterium Tuberculosis. Embo J., 25:1436-, 2006 Cited by PubMed Abstract: Cell envelope lipids play an important role in the pathogenicity of mycobacteria, but the mechanisms by which they are transported to the outer membrane of these prokaryotes are largely unknown. Here, we provide evidence that LppX is a lipoprotein required for the translocation of complex lipids, the phthiocerol dimycocerosates (DIM), to the outer membrane of Mycobacterium tuberculosis. Abolition of DIM transport following disruption of the lppX gene is accompanied by an important attenuation of the virulence of the tubercle bacillus. The crystal structure of LppX unveils an U-shaped beta-half-barrel dominated by a large hydrophobic cavity suitable to accommodate a single DIM molecule. LppX shares a similar fold with the periplasmic molecular chaperone LolA and the outer membrane lipoprotein LolB, which are involved in the localization of lipoproteins to the outer membrane of Gram-negative bacteria. Based on the structure and although an indirect participation of LppX in DIM transport cannot yet be ruled out, we propose LppX to be the first characterized member of a family of structurally related lipoproteins that carry lipophilic molecules across the mycobacterial cell envelope. PubMed: 16541102DOI: 10.1038/SJ.EMBOJ.7601048 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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