2byo
From Proteopedia
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CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS LIPOPROTEIN LPPX (RV2945C)
Overview
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 ... [(full description)]
About this Structure
2BYO is a [Single protein] structure of sequence from [Mycobacterium tuberculosis] with ZN, ACT, OAA, MLT, HXA and LNL as [ligands]. Full crystallographic information is available from [OCA].
Reference
LppX is a lipoprotein required for the translocation of phthiocerol dimycocerosates to the surface of Mycobacterium tuberculosis., 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, EMBO J. 2006 Apr 5;25(7):1436-44. Epub 2006 Mar 16. PMID:16541102
Page seeded by OCA on Mon Oct 29 20:02:47 2007
Categories: Mycobacterium tuberculosis | Single protein | Bourne, Y. | Canaan, S. | Gicquel, B. | Maurin, D. | Roig-Zamboni, V. | Sulzenbacher, G. | ACT | HXA | LNL | MLT | OAA | ZN | Lipid transport | Lipoprotein | Membrane | Palmitate
