1dts: Difference between revisions

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[[Image:1dts.gif|left|200px]]<br /><applet load="1dts" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1dts.gif|left|200px]]<br /><applet load="1dts" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1dts, resolution 1.65Å" />

'''CRYSTAL STRUCTURE OF AN ATP DEPENDENT CARBOXYLASE, DETHIOBIOTIN SYNTHASE, AT 1.65 ANGSTROMS RESOLUTION'''<br />

==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.

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 [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Dethiobiotin_synthase Dethiobiotin synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.3.3 6.3.3.3] Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1DTS OCA].

1DTS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Dethiobiotin_synthase Dethiobiotin synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.3.3 6.3.3.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DTS OCA].

==Reference==

Line 19:

[[Category: cyclo-ligase]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov~~ 20 13:~~34:23 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:20:20 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1dts.gif|left|200px]]<br /><applet load="1dts" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1dts.gif|left|200px]]<br /><applet load="1dts" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1dts, resolution 1.65&Aring;" />
 '''CRYSTAL STRUCTURE OF AN ATP DEPENDENT CARBOXYLASE, DETHIOBIOTIN SYNTHASE, AT 1.65 ANGSTROMS RESOLUTION'''<br />
 ==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.
+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==
-DTS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Dethiobiotin_synthase Dethiobiotin synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.3.3 6.3.3.3] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DTS OCA].
+DTS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Dethiobiotin_synthase Dethiobiotin synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.3.3 6.3.3.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DTS OCA].
 ==Reference==
@@ Line 19: / Line 19: @@
 [[Category: cyclo-ligase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:34:23 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:20:20 2008''