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4C47

Salmonella enterica trimeric lipoprotein SadB

Summary for 4C47
Entry DOI10.2210/pdb4c47/pdb
Related4C46
DescriptorINNER MEMBRANE LIPOPROTEIN (2 entities in total)
Functional Keywordscell adhesion, bacterial adhesion, membrane trafficking, membrane insertion, autotransport, polar core residues
Biological sourceSALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR TYPHIMURIUM STR. LT2
Total number of polymer chains3
Total formula weight71197.08
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 citationGrin, 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: 24369174
DOI: 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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건을2024-11-06부터공개중

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