2qlp: Difference between revisions

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[[Image:2qlp.jpg|left|200px]]
[[Image:2qlp.jpg|left|200px]]


{{Structure
<!--
|PDB= 2qlp |SIZE=350|CAPTION= <scene name='initialview01'>2qlp</scene>, resolution 2.47&Aring;
The line below this paragraph, containing "STRUCTURE_2qlp", creates the "Structure Box" on the page.
|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>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
|LIGAND= <scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY= <span class='plainlinks'>[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] </span>
or leave the SCENE parameter empty for the default display.
|GENE= dcd ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis])
-->
|DOMAIN=
{{STRUCTURE_2qlp|  PDB=2qlp |  SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qlp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qlp OCA], [http://www.ebi.ac.uk/pdbsum/2qlp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2qlp RCSB]</span>
}}


'''Bifunctional dCTP deaminase:dUTPase from Mycobacterium tuberculosis, apo form'''
'''Bifunctional dCTP deaminase:dUTPase from Mycobacterium tuberculosis, apo form'''
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[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: dCTP deaminase]]
[[Category: DCTP deaminase]]
[[Category: Christophersen, S.]]
[[Category: Christophersen, S.]]
[[Category: Harris, P.]]
[[Category: Harris, P.]]
[[Category: Willemoes, M.]]
[[Category: Willemoes, M.]]
[[Category: distorted beta barrel]]
[[Category: Distorted beta barrel]]
[[Category: hydrolase]]
[[Category: Hydrolase]]
[[Category: nucleotide metabolism]]
[[Category: Nucleotide metabolism]]
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:50:36 2008''

Revision as of 15:10, 4 May 2008

File:2qlp.jpg

Template:STRUCTURE 2qlp

Bifunctional dCTP deaminase:dUTPase from Mycobacterium tuberculosis, apo form


OverviewOverview

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 StructureAbout this Structure

2QLP is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

ReferenceReference

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 Page seeded by OCA on Sun May 4 15:10:00 2008

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