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4DZ1

Crystal structure of DalS, an ATP binding cassette transporter for D-alanine from Salmonella enterica

Summary for 4DZ1
Entry DOI10.2210/pdb4dz1/pdb
DescriptorDalS D-Alanine transporter, D-ALANINE (3 entities in total)
Functional Keywordsd-alanine binding, periplasmic, transport protein
Biological sourceSalmonella enterica
Total number of polymer chains1
Total formula weight29858.73
Authors
Mok, M.,Junop, M. (deposition date: 2012-02-29, release date: 2012-03-21, Last modification date: 2024-10-30)
Primary citationOsborne, S.E.,Tuinema, B.R.,Mok, M.C.,Lau, P.S.,Bui, N.K.,Tomljenovic-Berube, A.M.,Vollmer, W.,Zhang, K.,Junop, M.,Coombes, B.K.
Characterization of DalS, an ATP-binding Cassette Transporter for D-Alanine, and Its Role in Pathogenesis in Salmonella enterica.
J.Biol.Chem., 287:15242-15250, 2012
Cited by
PubMed Abstract: Expansion into new host niches requires bacterial pathogens to adapt to changes in nutrient availability and to evade an arsenal of host defenses. Horizontal acquisition of Salmonella Pathogenicity Island (SPI)-2 permitted the expansion of Salmonella enterica serovar Typhimurium into the intracellular environment of host cells by allowing it to deliver bacterial effector proteins across the phagosome membrane. This is facilitated by the SsrA-SsrB two-component regulatory system and a type III secretion system encoded within SPI-2. SPI-2 acquisition was followed by evolution of existing regulatory DNA, creating an expanded SsrB regulon involved in intracellular fitness and host infection. Here, we identified an SsrB-regulated operon comprising an ABC transporter in Salmonella. Biochemical and structural studies determined that the periplasmic solute-binding component, STM1633/DalS, transports D-alanine and that DalS is required for intracellular survival of the bacteria and for fitness in an animal host. This work exemplifies the role of nutrient exchange at the host-pathogen interface as a critical determinant of disease outcome.
PubMed: 22418438
DOI: 10.1074/jbc.M112.348227
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

227111

数据于2024-11-06公开中

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