Protein Science
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Cook, W. J.
Right arrow Articles by Chattopadhyay, D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Cook, W. J.
Right arrow Articles by Chattopadhyay, D.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Protein Science, Vol 9, Issue 4 704-712, Copyright © 2000 by The Protein Society

JOURNAL ARTICLE

Crystal structure of adenosine kinase from Toxoplasma gondii at 1.8 A resolution

WJ Cook, LJ DeLucas and D Chattopadhyay
Department of Pathology, University of Alabama at Birmingham, 35294, USA.

Human infection with Toxoplasma gondii is an important cause of morbidity and mortality. Protozoan parasites such as T. gondii are incapable of de novo purine biosynthesis and must acquire purines from their host, so the purine salvage pathway offers a number of potential targets for antiparasitic chemotherapy. In T. gondii tachyzoites, adenosine is the predominantly salvaged purine nucleoside, and thus adenosine kinase is a key enzyme in the purine salvage pathway of this parasite. The structure of T. gondii adenosine kinase was solved using molecular replacement and refined by simulated annealing at 1.8 A resolution to an R-factor of 0.214. The overall structure and the active site geometry are similar to human adenosine kinase, although there are significant differences. The T. gondii adenosine kinase has several unique features compared to the human sequence, including a five-residue deletion in one of the four linking segments between the two domains, which is probably responsible for a major change in the orientation of the two domains with respect to each other. These structural differences suggest the possibility of developing specific inhibitors of the parasitic enzyme.
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 Antimicrob. Agents Chemother.Home page
A. Luscher, P. Onal, A.-M. Schweingruber, and P. Maser
Adenosine Kinase of Trypanosoma brucei and Its Role in Susceptibility to Adenosine Antimetabolites
Antimicrob. Agents Chemother., November 1, 2007; 51(11): 3895 - 3901.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. C. M. Reddy, S. K. Palaninathan, N. D. Shetty, J. L. Owen, M. D. Watson, and J. C. Sacchettini
High Resolution Crystal Structures of Mycobacterium tuberculosis Adenosine Kinase: INSIGHTS INTO THE MECHANISM AND SPECIFICITY OF THIS NOVEL PROKARYOTIC ENZYME
J. Biol. Chem., September 14, 2007; 282(37): 27334 - 27342.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
L. Miallau, W. N. Hunter, S. M. McSweeney, and G. A. Leonard
Structures of Staphylococcus aureus D-Tagatose-6-phosphate Kinase Implicate Domain Motions in Specificity and Mechanism
J. Biol. Chem., July 6, 2007; 282(27): 19948 - 19957.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2000 by The Protein Society.