2byo
From Proteopedia
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|PDB= 2byo |SIZE=350|CAPTION= <scene name='initialview01'>2byo</scene>, resolution 2.15Å | |PDB= 2byo |SIZE=350|CAPTION= <scene name='initialview01'>2byo</scene>, resolution 2.15Å | ||
|SITE= <scene name='pdbsite=AC1:Mlt+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Mlt+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=HXA:DOCOSA-4,7,10,13,16,19-HEXAENOIC+ACID'>HXA</scene>, <scene name='pdbligand=LNL:ALPHA-LINOLENIC+ACID'>LNL</scene>, <scene name='pdbligand=MLT:MALATE+ION'>MLT</scene>, <scene name='pdbligand=OAA:OXALOACETATE+ION'>OAA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2byo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2byo OCA], [http://www.ebi.ac.uk/pdbsum/2byo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2byo RCSB]</span> | ||
}} | }} | ||
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[[Category: Roig-Zamboni, V.]] | [[Category: Roig-Zamboni, V.]] | ||
[[Category: Sulzenbacher, G.]] | [[Category: Sulzenbacher, G.]] | ||
| - | [[Category: ACT]] | ||
| - | [[Category: HXA]] | ||
| - | [[Category: LNL]] | ||
| - | [[Category: MLT]] | ||
| - | [[Category: OAA]] | ||
| - | [[Category: ZN]] | ||
[[Category: lipid transport]] | [[Category: lipid transport]] | ||
[[Category: lipoprotein]] | [[Category: lipoprotein]] | ||
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[[Category: palmitate]] | [[Category: palmitate]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:13:43 2008'' |
Revision as of 23:13, 30 March 2008
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| , resolution 2.15Å | |||||||
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| Sites: | |||||||
| Ligands: | , , , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 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.
About this Structure
2BYO is a Single protein structure of sequence from Mycobacterium tuberculosis. 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
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