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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
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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


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