1e2d: Difference between revisions

Revision as of 00:01, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1e2d.png

Template:STRUCTURE 1e2d

HUMAN THYMIDYLATE KINASE COMPLEXED WITH THYMIDINE MONOPHOSPHATE, ADENOSINE DIPHOSPHATE AND A MAGNESIUM-IONHUMAN THYMIDYLATE KINASE COMPLEXED WITH THYMIDINE MONOPHOSPHATE, ADENOSINE DIPHOSPHATE AND A MAGNESIUM-ION

Template:ABSTRACT PUBMED 10873853

About this StructureAbout this Structure

1E2D is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Insights into the phosphoryltransfer mechanism of human thymidylate kinase gained from crystal structures of enzyme complexes along the reaction coordinate., Ostermann N, Schlichting I, Brundiers R, Konrad M, Reinstein J, Veit T, Goody RS, Lavie A, Structure. 2000 Jun 15;8(6):629-42. PMID:10873853

Page seeded by OCA on Tue Jul 1 00:01:58 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1e2d.gif|left|200px]]
+{{Seed}}
+[[Image:1e2d.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1e2d|  PDB=1e2d  |  SCENE=  }}
-'''HUMAN THYMIDYLATE KINASE COMPLEXED WITH THYMIDINE MONOPHOSPHATE, ADENOSINE DIPHOSPHATE AND A MAGNESIUM-ION'''
+===HUMAN THYMIDYLATE KINASE COMPLEXED WITH THYMIDINE MONOPHOSPHATE, ADENOSINE DIPHOSPHATE AND A MAGNESIUM-ION===
-==Overview==
+<!--
-BACKGROUND: Thymidylate kinase (TMPK) is a nucleoside monophosphate kinase that catalyzes the reversible phosphoryltransfer between ATP and TMP to yield ADP and TDP. In addition to its vital role in supplying precursors for DNA synthesis, human TMPK has an important medical role participating in the activation of a number of anti-HIV prodrugs. RESULTS: Crystal structures of human TMPK in complex with TMP and ADP, TMP and the ATP analog AppNHp, TMP with ADP and the phosphoryl analog AlF(3), TDP and ADP, and the bisubstrate analog TP(5)A were determined. The conformations of the P-loop, the LID region, and the adenine-binding loop vary according to the nature of the complex. Substitution of ADP by AppNHp results in partial closure of the P-loop and the rotation of the TMP phosphate group to a catalytically unfavorable position, which rotates back in the AlF(3) complex to a position suitable for in-line attack. In the fully closed state observed in the TP(5)A and the TDP-ADP complexes, Asp15 interacts strongly with the 3'-hydroxyl group of TMP. CONCLUSIONS: The observed changes of nucleotide state and conformation and the corresponding protein structural changes are correlated with intermediates occurring along the reaction coordinate and show the sequence of events occurring during phosphate transfer. The low catalytic activity of human TMPK appears to be determined by structural changes required to achieve catalytic competence and it is suggested that a mechanism might exist to accelerate the activity.
+The line below this paragraph, {{ABSTRACT_PUBMED_10873853}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10873853 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10873853}}
 ==About this Structure==
@@ Line 33: / Line 37: @@
 [[Category: P-loop]]
 [[Category: Thymidylate kinase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:34:23 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 00:01:58 2008''