4GZE

Crystal structure of 6-phospho-beta-glucosidase from Lactobacillus plantarum (apo form)

4GZE の概要

• エントリーDOI: 10.2210/pdb4gze/pdb
• 関連するPDBエントリー: 3qom
• 分子名称: 6-phospho-beta-glucosidase, CHLORIDE ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: structural genomics, psi-biology, midwest center for structural genomics, mcsg, glycoside hydrolase, family 1, hydrolase
• 由来する生物種: Lactobacillus plantarum
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 335137.20

構造登録者

Michalska, K.,Hatzos-Skintges, C.,Bearden, J.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (登録日: 2012-09-06, 公開日: 2012-09-26, 最終更新日: 2024-11-20)

主引用文献

Michalska, K.,Tan, K.,Li, H.,Hatzos-Skintges, C.,Bearden, J.,Babnigg, G.,Joachimiak, A.
GH1-family 6-P-beta-glucosidases from human microbiome lactic acid bacteria.
Acta Crystallogr.,Sect.D, 69:451-463, 2013

PubMed Abstract: In lactic acid bacteria and other bacteria, carbohydrate uptake is mostly governed by phosphoenolpyruvate-dependent phosphotransferase systems (PTSs). PTS-dependent translocation through the cell membrane is coupled with phosphorylation of the incoming sugar. After translocation through the bacterial membrane, the β-glycosidic bond in 6'-P-β-glucoside is cleaved, releasing 6-P-β-glucose and the respective aglycon. This reaction is catalyzed by 6-P-β-glucosidases, which belong to two glycoside hydrolase (GH) families: GH1 and GH4. Here, the high-resolution crystal structures of GH1 6-P-β-glucosidases from Lactobacillus plantarum (LpPbg1) and Streptococcus mutans (SmBgl) and their complexes with ligands are reported. Both enzymes show hydrolytic activity towards 6'-P-β-glucosides. The LpPbg1 structure has been determined in an apo form as well as in a complex with phosphate and a glucose molecule corresponding to the aglycon molecule. The S. mutans homolog contains a sulfate ion in the phosphate-dedicated subcavity. SmBgl was also crystallized in the presence of the reaction product 6-P-β-glucose. For a mutated variant of the S. mutans enzyme (E375Q), the structure of a 6'-P-salicin complex has also been determined. The presence of natural ligands enabled the definition of the structural elements that are responsible for substrate recognition during catalysis.

PubMed: 23519420
DOI: 10.1107/S0907444912049608

実験手法

X-RAY DIFFRACTION (2.31 Å)