4C47
Salmonella enterica trimeric lipoprotein SadB
Summary for 4C47
Entry DOI | 10.2210/pdb4c47/pdb |
Related | 4C46 |
Descriptor | INNER MEMBRANE LIPOPROTEIN (2 entities in total) |
Functional Keywords | cell adhesion, bacterial adhesion, membrane trafficking, membrane insertion, autotransport, polar core residues |
Biological source | SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR TYPHIMURIUM STR. LT2 |
Total number of polymer chains | 3 |
Total formula weight | 71197.08 |
Authors | Grin, I.,Linke, D.,Hartmann, M.D. (deposition date: 2013-09-02, release date: 2014-01-08, Last modification date: 2024-05-08) |
Primary citation | Grin, I.,Hartmann, M.D.,Sauer, G.,Hernandez Alvarez, B.,Schutz, M.,Madlung, J.,Macek, B.,Felipe-Lopez, A.,Hensel, M.,Lupas, A.,Linke, D. A Trimeric Lipoprotein Assists in Trimeric Autotransporter Biogenesis in Enterobacteria. J.Biol.Chem., 289:7388-, 2014 Cited by PubMed Abstract: Trimeric autotransporter adhesins (TAAs) are important virulence factors of many Gram-negative bacterial pathogens. TAAs form fibrous, adhesive structures on the bacterial cell surface. Their N-terminal extracellular domains are exported through a C-terminal membrane pore; the insertion of the pore domain into the bacterial outer membrane follows the rules of β-barrel transmembrane protein biogenesis and is dependent on the essential Bam complex. We have recently described the full fiber structure of SadA, a TAA of unknown function in Salmonella and other enterobacteria. In this work, we describe the structure and function of SadB, a small inner membrane lipoprotein. The sadB gene is located in an operon with sadA; orthologous operons are only found in enterobacteria, whereas other TAAs are not typically associated with lipoproteins. Strikingly, SadB is also a trimer, and its co-expression with SadA has a direct influence on SadA structural integrity. This is the first report of a specific export factor of a TAA, suggesting that at least in some cases TAA autotransport is assisted by additional periplasmic proteins. PubMed: 24369174DOI: 10.1074/JBC.M113.513275 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.448 Å) |
Structure validation
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