2R60

Structure of apo Sucrose Phosphate Synthase (SPS) of Halothermothrix orenii

2R60 の概要

• エントリーDOI: 10.2210/pdb2r60/pdb
• 関連するPDBエントリー: 2R66 2R68
• 分子名称: Glycosyl transferase, group 1 (2 entities in total)
• 機能のキーワード: rossmann-fold, transferase
• 由来する生物種: Halothermothrix orenii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 56882.74

構造登録者

Sivaraman, J.,Chua, T.K. (登録日: 2007-09-05, 公開日: 2008-06-10, 最終更新日: 2024-03-13)

主引用文献

Chua, T.K.,Bujnicki, J.M.,Tan, T.C.,Huynh, F.,Patel, B.K.,Sivaraman, J.
The Structure of Sucrose Phosphate Synthase from Halothermothrix orenii Reveals Its Mechanism of Action and Binding Mode.
Plant Cell, 20:1059-1072, 2008

PubMed Abstract: Sucrose phosphate synthase (SPS) catalyzes the transfer of a glycosyl group from an activated donor sugar, such as uridine diphosphate glucose (UDP-Glc), to a saccharide acceptor D-fructose 6-phosphate (F6P), resulting in the formation of UDP and D-sucrose-6'-phosphate (S6P). This is a central regulatory process in the production of sucrose in plants, cyanobacteria, and proteobacteria. Here, we report the crystal structure of SPS from the nonphotosynthetic bacterium Halothermothrix orenii and its complexes with the substrate F6P and the product S6P. SPS has two distinct Rossmann-fold domains with a large substrate binding cleft at the interdomain interface. Structures of two complexes show that both the substrate F6P and the product S6P bind to the A-domain of SPS. Based on comparative analysis of the SPS structure with other related enzymes, the donor substrate, nucleotide diphosphate glucose, binds to the B-domain of SPS. Furthermore, we propose a mechanism of catalysis by H. orenii SPS. Our findings indicate that SPS from H. orenii may represent a valid model for the catalytic domain of plant SPSs and thus may provide useful insight into the reaction mechanism of the plant enzyme.

PubMed: 18424616
DOI: 10.1105/tpc.107.051193

実験手法

X-RAY DIFFRACTION (1.8 Å)