2qlp
From Proteopedia
(New page: 200px<br /><applet load="2qlp" size="350" color="white" frame="true" align="right" spinBox="true" caption="2qlp, resolution 2.47Å" /> '''Bifunctional dCTP de...) |
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| - | [[Image:2qlp.jpg|left|200px]] | + | [[Image:2qlp.jpg|left|200px]] |
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| - | '''Bifunctional dCTP deaminase:dUTPase from Mycobacterium tuberculosis, apo form''' | + | {{Structure |
| + | |PDB= 2qlp |SIZE=350|CAPTION= <scene name='initialview01'>2qlp</scene>, resolution 2.47Å | ||
| + | |SITE= <scene name='pdbsite=AC1:1pe+Binding+Site+For+Residue+E+162'>AC1</scene>, <scene name='pdbsite=AC2:1pe+Binding+Site+For+Residue+A+162'>AC2</scene>, <scene name='pdbsite=AC3:1pe+Binding+Site+For+Residue+C+162'>AC3</scene>, <scene name='pdbsite=AC4:1pe+Binding+Site+For+Residue+D+162'>AC4</scene>, <scene name='pdbsite=AC5:1pe+Binding+Site+For+Residue+B+162'>AC5</scene> and <scene name='pdbsite=AC6:1pe+Binding+Site+For+Residue+F+162'>AC6</scene> | ||
| + | |LIGAND= <scene name='pdbligand=1PE:PENTAETHYLENE GLYCOL'>1PE</scene> | ||
| + | |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] | ||
| + | |GENE= dcd ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis]) | ||
| + | }} | ||
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| + | '''Bifunctional dCTP deaminase:dUTPase from Mycobacterium tuberculosis, apo form''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2QLP is a [ | + | 2QLP 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=2QLP OCA]. |
==Reference== | ==Reference== | ||
| - | 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:// | + | 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] |
[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: nucleotide metabolism]] | [[Category: nucleotide metabolism]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:27:05 2008'' |
Revision as of 16:27, 20 March 2008
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| , resolution 2.47Å | |||||||
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| Sites: | , , , , and | ||||||
| Ligands: | |||||||
| Gene: | dcd (Mycobacterium tuberculosis) | ||||||
| Activity: | dCTP deaminase, with EC number 3.5.4.13 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Bifunctional dCTP deaminase:dUTPase from Mycobacterium tuberculosis, apo form
Overview
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.
About this Structure
2QLP is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.
Reference
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
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