This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2qlp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2qlp.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2qlp.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2qlp| PDB=2qlp | SCENE= }}
{{STRUCTURE_2qlp| PDB=2qlp | SCENE= }}
-
'''Bifunctional dCTP deaminase:dUTPase from Mycobacterium tuberculosis, apo form'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_18164314}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 18164314 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_18164314}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Nucleotide metabolism]]
[[Category: Nucleotide metabolism]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 15:10:00 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:55:27 2008''

Revision as of 16:55, 28 July 2008

Image:2qlp.png

Template:STRUCTURE 2qlp

Bifunctional dCTP deaminase:dUTPase from Mycobacterium tuberculosis, apo form

Template:ABSTRACT PUBMED 18164314

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

Page seeded by OCA on Mon Jul 28 19:55:27 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2qlp"
Personal tools