3OHR

Crystal structure of fructokinase from bacillus subtilis complexed with ADP

「3EPQ」から置き換えられました

3OHR の概要

• エントリーDOI: 10.2210/pdb3ohr/pdb
• 関連するPDBエントリー: 1XC3 3LM9
• 分子名称: Putative fructokinase, ADENOSINE-5'-DIPHOSPHATE, ZINC ION, ... (5 entities in total)
• 機能のキーワード: metal dependent, adp binding, d-fructose binding, structural genomics, psi-2, protein structure initiative, midwest center for structural genomics, mcsg, rok family, fructokinase, reductive methylation, transferase
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34020.88

構造登録者

Nocek, B.,Volkart, L.,Cuff, M.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (登録日: 2010-08-17, 公開日: 2010-09-15, 最終更新日: 2025-03-26)

主引用文献

Nocek, B.,Stein, A.J.,Jedrzejczak, R.,Cuff, M.E.,Li, H.,Volkart, L.,Joachimiak, A.
Structural studies of ROK fructokinase YdhR from Bacillus subtilis: insights into substrate binding and fructose specificity.
J.Mol.Biol., 406:325-342, 2011

PubMed Abstract: The main pathway of bacterial sugar phosphorylation utilizes specific phosphoenolpyruvate phosphotransferase system (PTS) enzymes. In addition to the classic PTS system, a PTS-independent secondary system has been described in which nucleotide-dependent sugar kinases are used for monosaccharide phosphorylation. Fructokinase (FK), which phosphorylates d-fructose with ATP as a cofactor, has been shown to be a member of this secondary system. Bioinformatic analysis has shown that FK is a member of the "ROK" (bacterial Repressors, uncharacterized Open reading frames, and sugar Kinases) sequence family. In this study, we report the crystal structures of ROK FK from Bacillus subtilis (YdhR) (a) apo and in the presence of (b) ADP and (c) ADP/d-fructose. All structures show that YdhR is a homodimer with a monomer composed of two similar α/β domains forming a large cleft between domains that bind ADP and D-fructose. Enzymatic activity assays support YdhR function as an ATP-dependent fructose kinase.

PubMed: 21185308
DOI: 10.1016/j.jmb.2010.12.021

実験手法

X-RAY DIFFRACTION (1.66 Å)