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


     

Protein Science (2004), 13:2547-2552. Published by Cold Spring Harbor Laboratory Press. Copyright © 2004 The Protein Society
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
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 Morris, V. K.
Right arrow Articles by Izard, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Morris, V. K.
Right arrow Articles by Izard, T.
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?

FOR THE RECORD

Substrate-induced asymmetry and channel closure revealed by the apoenzyme structure of Mycobacterium tuberculosis phosphopantetheine adenylyltransferase

Van K. Morris and Tina Izard

Department of Hematology-Oncology, St. Jude Children’s Research Hospital, Memphis, Tennessee 38105, USA

(RECEIVED April 15, 2004; FINAL REVISION June 1, 2004; ACCEPTED June 2, 2004)

Phosphopantetheine adenylyltransferase (PPAT) catalyzes the penultimate step in prokaryotic coenzyme A (CoA) biosynthesis, directing the transfer of an adenylyl group from ATP to 4'-phosphopantetheine (Ppant) to yield dephospho-CoA (dPCoA). The crystal structures of Escherichia coli PPAT bound to its substrates, product, and inhibitor revealed an allosteric hexameric enzyme with half-of-sites reactivity, and established an in-line displacement catalytic mechanism. To provide insight into the mechanism of ligand binding we solved the apoenzyme (Apo) crystal structure of PPAT from Mycobacterium tuberculosis. In its Apo form, PPAT is a symmetric hexamer with an open solvent channel. However, ligand binding provokes asymmetry and alters the structure of the solvent channel, so that ligand binding becomes restricted to one trimer.

Keywords: phosphopantetheine adenylyltransferase; apoenzyme; coenzyme A; tuberculosis; X-ray structure

Article and publication are at http://www.proteinscience.org/cgi/doi/10.1110/ps.04816904.

Reprint request to: Tina Izard, Department of Hematology-Oncology, St. Jude Children’s Research Hospital, Memphis TN 38105, USA; e-mail: tina.izard{at}stjude.org; fax: (901) 495-4981.


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
 J. Bacteriol.Home page
J. R. Miller, J. Ohren, R. W. Sarver, W. T. Mueller, P. d. Dreu, H. Case, and V. Thanabal
Phosphopantetheine Adenylyltransferase from Escherichia coli: Investigation of the Kinetic Mechanism and Role in Regulation of Coenzyme A Biosynthesis
J. Bacteriol., November 15, 2007; 189(22): 8196 - 8205.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2004 by The Protein Society.