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- W2071782537 abstract "Background In Escherichia coli, the enzymes of the biotin biosynthesis pathway are encoded by the bio operon. One of these enzymes, ATP-dependent dethiobiotin synthetase, catalyzes the carboxylation of 7,8-diaminopelargonic acid leading to the formation of the ureido ring of biotin. The enzyme belongs to the class of ATP-dependent carboxylases and we present here the first crystal structure determined for this class of enzyme.Results We have determined the crystal structure of homodimeric dethiobiotin synthetase to 1.65 å resolution. The subunit consists of a seven-stranded parallel β -sheet, surrounded by α -helices. The sheet contains the classical mononucleotide-binding motif with a fingerprint peptide Gly-X-X-X-X-X-Gly-Lys-Thr. The mononucleotide binding part of the structure is very similar to the GTP-binding protein H- ras -p21 and thus all GTP-binding proteins. A comparison reveals that some of the residues, which in H- ras -p21 interact with the nucleotide and the metal ion, are conserved in the synthetase.Conclusions The three-dimensional structure of dethiobiotin synthetase has revealed that ATP-dependent carboxylases contain the classical mononucleotide-binding fold. Considerable similarities to the structure of the GTP-binding protein H- ras -p21 were found, indicating that both proteins might have evolved from a common ancestral mononucleotide-binding fold." @default.
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- W2071782537 date "1994-05-01" @default.
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- W2071782537 title "Crystal structure of an ATP-dependent carboxylase, dethiobiotin synthetase, at 1.65 å resolution" @default.
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- W2071782537 doi "https://doi.org/10.1016/s0969-2126(00)00042-3" @default.
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