1dts

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:59, 7 February 2024) (edit) (undo)
 
(16 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1dts.gif|left|200px]]
 
-
{{Structure
+
==CRYSTAL STRUCTURE OF AN ATP DEPENDENT CARBOXYLASE, DETHIOBIOTIN SYNTHASE, AT 1.65 ANGSTROMS RESOLUTION==
-
|PDB= 1dts |SIZE=350|CAPTION= <scene name='initialview01'>1dts</scene>, resolution 1.65&Aring;
+
<StructureSection load='1dts' size='340' side='right'caption='[[1dts]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND=
+
<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>
-
|ACTIVITY= [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]
+
</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>
-
|GENE=
+
<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>
-
'''CRYSTAL STRUCTURE OF AN ATP DEPENDENT CARBOXYLASE, DETHIOBIOTIN SYNTHASE, AT 1.65 ANGSTROMS RESOLUTION'''
+
==See Also==
-
 
+
*[[Dethiobiotin synthetase 3D structures|Dethiobiotin synthetase 3D structures]]
-
 
+
== References ==
-
==Overview==
+
<references/>
-
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.
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
-
1DTS is a [[Single protein]] structure of sequence from [http://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].
+
-
 
+
-
==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:[http://www.ncbi.nlm.nih.gov/pubmed/8081756 8081756]
+
-
[[Category: Dethiobiotin synthase]]
+
[[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]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:44:10 2008''
+

Current revision

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

PDB ID 1dts

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1dts"
Personal tools