2qlp: Difference between revisions
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|PDB= 2qlp |SIZE=350|CAPTION= <scene name='initialview01'>2qlp</scene>, resolution 2.47Å | |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> | |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> | |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] | |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> | ||
|GENE= dcd ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis]) | |GENE= dcd ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis]) | ||
|DOMAIN= | |||
|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> | |||
}} | }} | ||
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[[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]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:50:36 2008'' | ||
Revision as of 04:50, 31 March 2008
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| , resolution 2.47Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , and | ||||||
| Ligands: | |||||||
| Gene: | dcd (Mycobacterium tuberculosis) | ||||||
| Activity: | dCTP deaminase, with EC number 3.5.4.13 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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