2vkj

Structure of the soluble domain of the membrane protein TM1634 from Thermotoga maritima

spinqualitylabelsall models 2vkj, resolution 1.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2vkj is a 2 chain structure with sequence from Thermotoga maritima. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.65Å Ligands: SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9X1W9_THEMA Publication Abstract from PubMed 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 Co(2+) were located, were identified using crystallography and NMR, respectively. Structure and ligand binding of the soluble domain of a Thermotoga maritima membrane protein of unknown function TM1634.,McCleverty CJ, Columbus L, Kreusch A, Lesley SA Protein Sci. 2008 Mar 27;. PMID:18369189 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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