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Structure and ligand binding of the soluble domain of a Thermotoga maritima membrane protein of unknown function TM1634
Author(s) -
McCleverty Clare J.,
Columbus Linda,
Kreusch Andreas,
Lesley Scott A.
Publication year - 2008
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.083432208
Subject(s) - thermotoga maritima , structural genomics , dimer , chemistry , membrane protein , protein structure , membrane , crystallography , biochemistry , stereochemistry , biology , gene , organic chemistry , escherichia coli
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 α‐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 Co 2+ were located, were identified using crystallography and NMR, respectively.