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


     

Published online before print March 27, 2008, 10.1110/ps.083432208
Protein Science (2008), 17:869-877. Published by Cold Spring Harbor Laboratory Press. Copyright © 2008 The Protein Society
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
ps.083432208v1
17/5/869    most recent
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
Google Scholar
Right arrow Articles by McCleverty, C. J.
Right arrow Articles by Lesley, S. A.
PubMed
Right arrow PubMed Citation
Right arrow Articles by McCleverty, C. J.
Right arrow Articles by Lesley, S. A.
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?

Structure and ligand binding of the soluble domain of a Thermotoga maritima membrane protein of unknown function TM1634

Clare J. McCleverty1,3, Linda Columbus2,3,4, Andreas Kreusch1, and Scott A. Lesley1,2

1 The Genomics Institute of the Novartis Research Foundation, San Diego, California 92121, USA
2 The Joint Center for Structural Genomics and The Scripps Research Institute, Department of Molecular Biology, La Jolla, California 92037, USA

(RECEIVED January 3, 2008; FINAL REVISION February 12, 2008; ACCEPTED February 12, 2008)

As a part of the Joint Center for Structural Genomics (JCSG) biological targets, the structures of soluble domains of membrane proteins from Thermotoga maritima were pursued. Here, we report the crystal structure of the soluble domain of TM1634, a putative membrane protein of 128 residues (15.1 kDa) and unknown function. The soluble domain of TM1634 is an {alpha}-helical dimer that contains a single tetratrico peptide repeat (TPR) motif in each monomer where each motif is similar to that found in Tom20. The overall fold, however, is unique and a DALI search does not identify similar folds beyond the 38-residue TPR motif. Two different putative ligand binding sites, in which PEG200 and Co2+ were located, were identified using crystallography and NMR, respectively.

Keywords: TPR motif; Thermotoga maritima ; Co2+ ligand; PEG binding site; membrane protein; protein of unknown function


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?




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2008 by The Protein Society.