Salmonella typhimurium structure

Hyde, C.C., et al. Three-dimensional structure of the tryptophan synthase az pz multienzyme complex from Salmonella typhimurium. J. Biol. Chem. 263 17857-17871, 1988. 

A great deal of our current understanding of the structure and function of the outer membrane of Gram-negative bacteria has come from studies with Escherichia coli and Salmonella typhimurium. The permeability barrier function of the outer membrane can... 

Using PTLC six major fractions of lipids (phospholipids, free sterols, free fatty acids, triacylglycerols, methyl esters, and sterol esters) were separated from the skin lipids of chicken to smdy the penetration responses of Schistosoma cercaria and Austrobilharzia variglandis [79a]. To determine the structure of nontoxic lipids in lipopolysaccharides of Salmonella typhimurium, monophosphoryl lipids were separated from these lipids using PTLC. The separated fractions were used in FAB-MS to determine [3-hydroxymyristic acid, lauric acid, and 3-hydroxymyristic acids [79b]. 

MacGregor, J. T. Jurd, L. Mutagenicity of plant flavonoids structural requirements for mutagenic activity in Salmonella typhimurium. Mutat. Res. 1978, 54, 297-309. 

Ultrasound (US) disrupts biological structures and may lead to death when applied with sufficient intensity (Betts and Everis, 2005). The use of ultrasound to disinfect fruit and vegetables has not been described frequently in the literature. The results from a study by Seymour et al. (2002) indicated that a combination of ultrasound and chlorinated water reduced the numbers of both Salmonella Typhimurium and E. coli from iceberg lettuce. However, the authors concluded that the cost of such a method is high and that the combination does not completely remove pathogens from fresh produce. Therefore, this is probably not a well-suited alternative method for the decontamination of fruit and vegetables. 

Forst, D., Welte, W., Wacker, T. and Diederichs, K. (1998). Structure of the sucrose-specific porin ScrY from Salmonella typhimurium and its complex with sucrose, Nature Struct. Biol., 5, 7-46. 

Meyer, J. E. W., Hofnung, M. and Schulz, G. E. (1997). Structure of maltoporin from Salmonella typhimurium ligated with a nitrophenyl-maltotrioside, J. Mol. Biol., 266, 761-775. 

C. R. H. Raetz, in C. Neidhardt, J. 1. Ingraham, K. Brooks Low, B. Magasanik, M. Schaechter, and H. E. Umbarger (Eds.), Escherichia coli and Salmonella typhimurium Cellular and Molecular Biology Structure and Biosynthesis of Lipid A, p. 498. American Society of Microbiologists, Washington DC, 1987. 

Romling, U., Bain, Z., Hammar, M., Sierralta, W. D., and Normark, S. (1998). Curli fibers are highly conserved between Salmonella typhimurium and Escherichia coli with respect to operon structure and regulation. /. Bacteriol. 180, 722-731. 

Bignami M, Cardamone, G, Comba P, et al. 1977. Relationship between chemical structure and mutagenic activity in some pesticides The use of Salmonella typhimurium and Aspergillus nidulans. Mutat Res 46 243-244. 

Jason Kindrachuk is a postdoctoral fellow at the University of British Columbia (UBC) in the laboratory of Professor R. E. W. Hancock. Jason received his Ph.D. from the University of Saskatchewan in 2007 where his research focused on host and pathogen sensory systems. During his study he specially focused on TLR-9 receptor—ligand interactions and the interactions between host defense peptides and the PhoPQ two-component sensory system of Salmonella typhimurium. In 2008 Jason received the Canadian Cystic Fibrosis Foundation Kin Canada Fellowship for his research in the area of alternative therapies for treatment of antibiotic- and multidrug-resistant bacteria. Currently his research is focused on the investigation of structure-activity relationships amongst natural and synthetic host defense peptides from the perspective of associated immunomodulatory activities and as well as vaccine formulation strategies. 

Shimizu N, Yasui Y, Matsumoto N. 1983. Structural specificity of aromatic compounds with special reference to mutagenic activity in Salmonella typhimurium - a series of chloro- or fluoro-nitrobenzene derivatives. Mutat Res 116 217-238. 

Spanggord RJ, Mortelmans KE, Griffin AF, et al. 1982b. Mutagenicity in Salmonella typhimurium and structure-activity relationships of wastewater components emanating from the manufacture of trinitrotoluene. Environ Mutagen 4 163-179. 

The main component of the adenosine diphosphate sugar fraction from a Salmonella typhimurium strain was unexpectedly found to be adenosine 5 -(D-mannitol 1-pyrophosphate)190 (45). Upon treatment with acid or with snake-venom pyrophosphatase, it produces adenosine 5 -phosphate and D-mannitol 1-phosphate these observations confirm the structure assigned. 

Thompson, T.B. Thomas, M.G. Escalante-Semerena, J.C. Rayment, L Three-dimensional structure of adenosylcobinamide kinase/adenosylcobina-mide phosphate guanylyltransferase from Salmonella typhimurium determined to 2.3 A resolution. Biochemistry, 37, 7686-7695 (1998)... 

LiCalsi, C. Crocenzi, T.S. Freire, E. Roseman, S. Sugar transport by the bacterial phosphotransferase system. Structural and thermodynamic domains of enzyme I of Salmonella typhimurium. J. Biol. Chem., 266, 19519-19527 (1991)... 

Liljestrom, P. Laamanen, I. Palva, E.T. Structure and expression of the ompB operon, the regulatory locus for the outer membrane porin regulon in Salmonella typhimurium LT-2. J. Mol. Biol., 201, 663-673 (1988)... 

Cheng, G. Bennett, E.M. Begley, T.P. Ealick, S.E. Crystal structure of 4-ami-no-5-hydroxymethyl-2-methylpyrimidine phosphate kinase from Salmonella typhimurium at 2.3 A resolution. Structure, 10, 225-235 (2002)... 

The structure of glutamine synthase from Salmonella typhimurium. The enzyme consists of twelve identical subunits arranged like a hexagonal prism, (a) View down the sixfold axis of symmetry. The top ring of monomers are alternately colored light and dark blue and the bottom ring of monomers light and dark red. The active sites of each monomer are marked by pairs of Mn"+ ions (white spheres). 

The L-rhamnulose 1-phosphate aldolase (RhuA EC 4.1.2.19) is found in the microbial degradation of L-rhamnose which, after conversion into the corresponding ketose 1-phosphate 44, is cleaved into 41 and L-lactaldehyde (l-16). The RhuA has been isolated from E. coli [336-339], and characterized as a metallo-protein [194,340,341]. Cloning was reported for the E. coli [342,343] and Salmonella typhimurium [344] genes, and construction of an efficient overexpression system [195,220] has set the stage for crystallization of the homotetrameric E. coli protein for the purposes of an X-ray structure analysis [345]. 

The structure of the lipopolysaccharide region from Salmonella typhimurium provides a good model system and is shown in Figure 1. The LPS is composed of four major components ... 

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