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New page: left|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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[[Image:1dts.gif|left|200px]]<br /><applet load="1dts" size="450" 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==
==CRYSTAL STRUCTURE OF AN ATP DEPENDENT CARBOXYLASE, DETHIOBIOTIN SYNTHASE, AT 1.65 ANGSTROMS RESOLUTION==
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.
<StructureSection load='1dts' size='340' side='right'caption='[[1dts]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1dts]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DTS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DTS FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dts OCA], [https://pdbe.org/1dts PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dts RCSB], [https://www.ebi.ac.uk/pdbsum/1dts PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dts ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BIOD1_ECOLI BIOD1_ECOLI] Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA) to form an ureido ring. Only CTP can partially replace ATP while diaminobiotin is only 37% as effective as 7,8-diaminopelargonic acid.<ref>PMID:4892372</ref> <ref>PMID:4921568</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dt/1dts_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dts ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
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].
*[[Dethiobiotin synthetase 3D structures|Dethiobiotin synthetase 3D structures]]
 
== References ==
==Reference==
<references/>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8081756 8081756]
__TOC__
[[Category: Dethiobiotin synthase]]
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Huang, W.]]
[[Category: Huang W]]
[[Category: Lindqvist, Y.]]
[[Category: Lindqvist Y]]
[[Category: Schneider, G.]]
[[Category: Schneider G]]
[[Category: cyclo-ligase]]
 
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