2VKO

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

Summary for 2VKO

• Entry DOI: 10.2210/pdb2vko/pdb
• Related: 2VKJ
• Descriptor: TM1634, TETRAETHYLENE GLYCOL, HEXAETHYLENE GLYCOL, ... (4 entities in total)
• Functional Keywords: sad, tpr motif, membrane protein, thermotoga maritima, structural genomics, jcsg, joint center for structural genomics
• Biological source: THERMOTOGA MARITIMA
• Total number of polymer chains: 4
• Total formula weight: 49689.14

Authors

McCleverty, C.J.,Columbus, L.,Kreusch, A.,Lesley, S.A.,Joint Center for Structural Genomics (JCSG) (deposition date: 2007-12-20, release date: 2008-04-08, Last modification date: 2023-12-13)

Primary citation

Mccleverty, C.J.,Columbus, L.,Kreusch, A.,Lesley, S.A.
Structure and Ligand Binding of the Soluble Domain of a Thermotoga Maritima Membrane Protein of Unknown Function Tm1634.
Protein Sci., 17:869-, 2008

PubMed Abstract: 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.

PubMed: 18369189
DOI: 10.1110/PS.083432208

Experimental method

X-RAY DIFFRACTION (1.79 Å)