1R7A

Sucrose Phosphorylase from Bifidobacterium adolescentis

1R7A の概要

• エントリーDOI: 10.2210/pdb1r7a/pdb
• 分子名称: sucrose phosphorylase, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL (3 entities in total)
• 機能のキーワード: beta-alpha-barrels, dimer, glycoside hydrolase, transferase
• 由来する生物種: Bifidobacterium adolescentis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 112813.62

構造登録者

Sprogoe, D.,van den Broek, L.A.M.,Mirza, O.,Kastrup, J.S.,Voragen, A.G.J.,Gajhede, M.,Skov, L.K. (登録日: 2003-10-21, 公開日: 2004-02-10, 最終更新日: 2024-11-20)

主引用文献

Sprogoe, D.,van den Broek, L.A.,Mirza, O.,Kastrup, J.S.,Voragen, A.G.,Gajhede, M.,Skov, L.K.
Crystal structure of sucrose phosphorylase from Bifidobacterium adolescentis.
Biochemistry, 43:1156-1162, 2004

PubMed Abstract: Around 80 enzymes are implicated in the generic starch and sucrose pathways. One of these enzymes is sucrose phosphorylase, which reversibly catalyzes the conversion of sucrose and orthophosphate to d-Fructose and alpha-d-glucose 1-phosphate. Here, we present the crystal structure of sucrose phosphorylase from Bifidobacterium adolescentis (BiSP) refined at 1.77 A resolution. It represents the first 3D structure of a sucrose phosphorylase and is the first structure of a phosphate-dependent enzyme from the glycoside hydrolase family 13. The structure of BiSP is composed of the four domains A, B, B', and C. Domain A comprises the (beta/alpha)(8)-barrel common to family 13. The catalytic active-site residues (Asp192 and Glu232) are located at the tips of beta-sheets 4 and 5 in the (beta/alpha)(8)-barrel, as required for family 13 members. The topology of the B' domain disfavors oligosaccharide binding and reduces the size of the substrate access channel compared to other family 13 members, underlining the role of this domain in modulating the function of these enzymes. It is remarkable that the fold of the C domain is not observed in any other known hydrolases of family 13. BiSP was found as a homodimer in the crystal, and a dimer contact surface area of 960 A(2) per monomer was calculated. The majority of the interactions are confined to the two B domains, but interactions between the loop 8 regions of the two barrels are also observed. This results in a large cavity in the dimer, including the entrance to the two active sites.

PubMed: 14756551
DOI: 10.1021/bi0356395

実験手法

X-RAY DIFFRACTION (1.77 Å)