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1dts

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{{STRUCTURE_1dts| PDB=1dts | SCENE= }}
{{STRUCTURE_1dts| PDB=1dts | SCENE= }}
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'''CRYSTAL STRUCTURE OF AN ATP DEPENDENT CARBOXYLASE, DETHIOBIOTIN SYNTHASE, AT 1.65 ANGSTROMS RESOLUTION'''
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===CRYSTAL STRUCTURE OF AN ATP DEPENDENT CARBOXYLASE, DETHIOBIOTIN SYNTHASE, AT 1.65 ANGSTROMS RESOLUTION===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_8081756}}
==About this Structure==
==About this Structure==
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[[Category: Schneider, G.]]
[[Category: Schneider, G.]]
[[Category: Cyclo-ligase]]
[[Category: Cyclo-ligase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:36:14 2008''

Revision as of 20:36, 30 June 2008

Image:1dts.png

Template:STRUCTURE 1dts

CRYSTAL STRUCTURE OF AN ATP DEPENDENT CARBOXYLASE, DETHIOBIOTIN SYNTHASE, AT 1.65 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 8081756

About this Structure

1DTS is a Single protein structure of sequence from Escherichia coli. 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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