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- W2040338718 abstract "Six putative ATP-binding motifs of SecA protein were altered by oligonucleotide-directed mutagenesis to try to define the ATP-binding regions of this multifunctional protein. The effects of the mutations were analysed by genetic and biochemical assays. The results show that SecA contains two essential ATP-binding domains. One domain is responsible for high-affinity ATP binding and contains motifs AO and BO, located at amino acid residues 102-109 and 198-210, respectively. A second domain is responsible for low-affinity ATP binding and contains motifs A3 and a predicted B motif located at amino acid residues 503-511 and 631-653, respectively. The ATP-binding properties of both domains were essential for SecA-dependent translocation ATPase and in vitro protein translocation activities. The significance of these findings for the mechanism of SecA-dependent protein translocation is discussed." @default.
- W2040338718 created "2016-06-24" @default.
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- W2040338718 creator A5047931883 @default.
- W2040338718 date "1993-11-01" @default.
- W2040338718 modified "2023-10-18" @default.
- W2040338718 title "Two distinct ATP-binding domains are needed to promote protein export by Escherichia coli SecA ATPase" @default.
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- W2040338718 doi "https://doi.org/10.1111/j.1365-2958.1993.tb00921.x" @default.
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