2VKO

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

2VKO の概要

• エントリーDOI: 10.2210/pdb2vko/pdb
• 関連するPDBエントリー: 2VKJ
• 分子名称: TM1634, TETRAETHYLENE GLYCOL, HEXAETHYLENE GLYCOL, ... (4 entities in total)
• 機能のキーワード: sad, tpr motif, membrane protein, thermotoga maritima, structural genomics, jcsg, joint center for structural genomics
• 由来する生物種: THERMOTOGA MARITIMA
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 49689.14

構造登録者

McCleverty, C.J.,Columbus, L.,Kreusch, A.,Lesley, S.A.,Joint Center for Structural Genomics (JCSG) (登録日: 2007-12-20, 公開日: 2008-04-08, 最終更新日: 2023-12-13)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.79 Å)