3AI7

Crystal Structure of Bifidobacterium Longum Phosphoketolase

3AI7 の概要

• エントリーDOI: 10.2210/pdb3ai7/pdb
• 分子名称: Xylulose-5-phosphate/fructose-6-phosphate phosphoketolase, THIAMINE DIPHOSPHATE, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: thiamine-diphosphate protein, lyase
• 由来する生物種: Bifidobacterium longum
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 751323.26

構造登録者

Takahashi, K.,Tagami, U.,Shimba, N.,Kashiwagi, T.,Ishikawa, K.,Suzuki, E. (登録日: 2010-05-10, 公開日: 2010-09-15, 最終更新日: 2024-04-03)

主引用文献

Takahashi, K.,Tagami, U.,Shimba, N.,Kashiwagi, T.,Ishikawa, K.,Suzuki, E.
Crystal structure of Bifidobacterium Longum phosphoketolase; key enzyme for glucose metabolism in Bifidobacterium
Febs Lett., 584:3855-3861, 2010

PubMed Abstract: The crystal structure of Bifidobacterium longum phosphoketolase, a thiamine diphosphate (TPP) dependent enzyme, has been determined at 2.2A resolution. The enzyme is a dimer with the active sites located at the interface between the two identical subunits with molecular mass of 92.5 kDa. The bound TPP is almost completely shielded from solvent except for the catalytically important C2-carbon of the thiazolium ring, which can be accessed by a substrate sugar through a narrow funnel-shaped channel. In silico docking studies of B. longum phosphoketolase with its substrate enable us to propose a model for substrate binding.

PubMed: 20674574
DOI: 10.1016/j.febslet.2010.07.043

実験手法

X-RAY DIFFRACTION (2.2 Å)