1dts
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(New page: 200px<br /><applet load="1dts" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dts, resolution 1.65Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 11:27, 20 November 2007
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CRYSTAL STRUCTURE OF AN ATP DEPENDENT CARBOXYLASE, DETHIOBIOTIN SYNTHASE, AT 1.65 ANGSTROMS RESOLUTION
Overview
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 A resolution. The subunit consists of a, seven-stranded parallel beta-sheet, surrounded by alpha-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.
About this Structure
1DTS is a Single protein structure of sequence from Escherichia coli. Active as Dethiobiotin synthase, with EC number 6.3.3.3 Full crystallographic information is available from OCA.
Reference
Crystal structure of an ATP-dependent carboxylase, dethiobiotin synthetase, at 1.65 A resolution., Huang W, Lindqvist Y, Schneider G, Gibson KJ, Flint D, Lorimer G, Structure. 1994 May 15;2(5):407-14. PMID:8081756
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