4c7x
Thiamine Pyrophosphate Bound Transketolase from Lactobacillus salivarius at 2.2A resolutionThiamine Pyrophosphate Bound Transketolase from Lactobacillus salivarius at 2.2A resolution
Structural highlights
FunctionPublication Abstract from PubMedProbiotic bacterial strains have been shown to enhance the health of the host through a range of mechanisms including colonization, resistance against pathogens, secretion of antimicrobial compounds and modulation of the activity of the innate immune system. Lactobacillus salivarius UCC118 is a well characterized probiotic strain which survives intestinal transit and has many desirable host-interaction properties. Probiotic bacteria display a wide range of catabolic activities, which determine their competitiveness in vivo. Some lactobacilli are heterofermentative and can metabolize pentoses, using a pathway in which transketolase and transaldolase are key enzymes. L. salivarius UCC118 is capable of pentose utilization because it encodes the key enzymes on a megaplasmid. The crystal structures of the megaplasmid-encoded transketolase with and without the enzyme cofactor thiamine pyrophosphate have been determined. Comparisons with other known transketolase structures reveal a high degree of structural conservation in both the catalytic site and the overall conformation. This work extends structural knowledge of the transketolases to the industrially and commercially important Lactobacillus genus. High-resolution structures of Lactobacillus salivarius transketolase in the presence and absence of thiamine pyrophosphate.,Lukacik P, Lobley CM, Bumann M, Arena de Souza V, Owens RJ, O'Toole PW, Walsh MA Acta Crystallogr F Struct Biol Commun. 2015 Oct 1;71(Pt 10):1327-34. doi:, 10.1107/S2053230X1501657X. Epub 2015 Sep 23. PMID:26457526[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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