2qxx

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[[Image:2qxx.jpg|left|200px]]
 
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{{Structure
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==Bifunctional dCTP deaminase: dUTPase from Mycobacterium tuberculosis in complex with dTTP==
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|PDB= 2qxx |SIZE=350|CAPTION= <scene name='initialview01'>2qxx</scene>, resolution 2.0&Aring;
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<StructureSection load='2qxx' size='340' side='right'caption='[[2qxx]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Residue+A+202'>AC1</scene>, <scene name='pdbsite=AC2:Mg+Binding+Site+For+Residue+B+202'>AC2</scene>, <scene name='pdbsite=AC3:Ttp+Binding+Site+For+Residue+A+201'>AC3</scene>, <scene name='pdbsite=AC4:Ttp+Binding+Site+For+Residue+B+201'>AC4</scene>, <scene name='pdbsite=AC5:1pe+Binding+Site+For+Residue+A+203'>AC5</scene>, <scene name='pdbsite=AC6:1pe+Binding+Site+For+Residue+B+203'>AC6</scene> and <scene name='pdbsite=AC7:1pe+Binding+Site+For+Residue+B+204'>AC7</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TTP:THYMIDINE-5&#39;-TRIPHOSPHATE'>TTP</scene> and <scene name='pdbligand=1PE:PENTAETHYLENE GLYCOL'>1PE</scene>
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<table><tr><td colspan='2'>[[2qxx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QXX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QXX FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/dCTP_deaminase dCTP deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.13 3.5.4.13]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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|GENE= dcd ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TTP:THYMIDINE-5-TRIPHOSPHATE'>TTP</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qxx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qxx OCA], [https://pdbe.org/2qxx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qxx RCSB], [https://www.ebi.ac.uk/pdbsum/2qxx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qxx ProSAT]</span></td></tr>
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</table>
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'''Bifunctional dCTP deaminase: dUTPase from Mycobacterium tuberculosis in complex with dTTP'''
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== Function ==
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[https://www.uniprot.org/uniprot/DCDB_MYCTU DCDB_MYCTU] Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate. It also acts as a dUTP diphosphatase. Affinity for dCTP and dUTP are very similar.<ref>PMID:18164314</ref>
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qx/2qxx_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2qxx ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
Recombinant deoxycytidine triphosphate (dCTP) deaminase from Mycobacterium tuberculosis was produced in Escherichia coli and purified. The enzyme proved to be a bifunctional dCTP deaminase:deoxyuridine triphosphatase. As such, the M. tuberculosis enzyme is the second bifunctional enzyme to be characterised and provides evidence for bifunctionality of dCTP deaminase occurring outside the Archaea kingdom. A steady-state kinetic analysis revealed that the affinity for dCTP and deoxyuridine triphosphate as substrates for the synthesis of deoxyuridine monophosphate were very similar, a result that contrasts that obtained previously for the archaean Methanocaldococcus jannaschii enzyme, which showed approximately 10-fold lower affinity for deoxyuridine triphosphate than for dCTP. The crystal structures of the enzyme in complex with the inhibitor, thymidine triphosphate, and the apo form have been solved. Comparison of the two shows that upon binding of thymidine triphosphate, the disordered C-terminal arranges as a lid covering the active site, and the enzyme adapts an inactive conformation as a result of structural changes in the active site. In the inactive conformation dephosphorylation cannot take place due to the absence of a water molecule otherwise hydrogen-bonded to O2 of the alpha-phosphate.
Recombinant deoxycytidine triphosphate (dCTP) deaminase from Mycobacterium tuberculosis was produced in Escherichia coli and purified. The enzyme proved to be a bifunctional dCTP deaminase:deoxyuridine triphosphatase. As such, the M. tuberculosis enzyme is the second bifunctional enzyme to be characterised and provides evidence for bifunctionality of dCTP deaminase occurring outside the Archaea kingdom. A steady-state kinetic analysis revealed that the affinity for dCTP and deoxyuridine triphosphate as substrates for the synthesis of deoxyuridine monophosphate were very similar, a result that contrasts that obtained previously for the archaean Methanocaldococcus jannaschii enzyme, which showed approximately 10-fold lower affinity for deoxyuridine triphosphate than for dCTP. The crystal structures of the enzyme in complex with the inhibitor, thymidine triphosphate, and the apo form have been solved. Comparison of the two shows that upon binding of thymidine triphosphate, the disordered C-terminal arranges as a lid covering the active site, and the enzyme adapts an inactive conformation as a result of structural changes in the active site. In the inactive conformation dephosphorylation cannot take place due to the absence of a water molecule otherwise hydrogen-bonded to O2 of the alpha-phosphate.
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==About this Structure==
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Mechanism of dTTP inhibition of the bifunctional dCTP deaminase:dUTPase encoded by Mycobacterium tuberculosis.,Helt SS, Thymark M, Harris P, Aagaard C, Dietrich J, Larsen S, Willemoes M J Mol Biol. 2008 Feb 15;376(2):554-69. Epub 2007 Dec 5. PMID:18164314<ref>PMID:18164314</ref>
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2QXX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QXX OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Mechanism of dTTP inhibition of the bifunctional dCTP deaminase:dUTPase encoded by Mycobacterium tuberculosis., Helt SS, Thymark M, Harris P, Aagaard C, Dietrich J, Larsen S, Willemoes M, J Mol Biol. 2008 Feb 15;376(2):554-69. Epub 2007 Dec 5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18164314 18164314]
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</div>
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[[Category: Mycobacterium tuberculosis]]
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<div class="pdbe-citations 2qxx" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: dCTP deaminase]]
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[[Category: Christophersen, S.]]
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[[Category: Harris, P.]]
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[[Category: Willemoes, M.]]
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[[Category: 1PE]]
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[[Category: MG]]
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[[Category: TTP]]
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[[Category: distorted beta barrel]]
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[[Category: hydrolase]]
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[[Category: nucleotide metabolism]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 15:47:07 2008''
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==See Also==
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*[[Deaminase 3D structures|Deaminase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Mycobacterium tuberculosis H37Rv]]
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[[Category: Christophersen S]]
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[[Category: Harris P]]
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[[Category: Willemoes M]]

Current revision

Bifunctional dCTP deaminase: dUTPase from Mycobacterium tuberculosis in complex with dTTP

PDB ID 2qxx

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