4F66

The crystal structure of 6-phospho-beta-glucosidase from Streptococcus mutans UA159 in complex with beta-D-glucose-6-phosphate.

Replaces:  4DDE

Summary for 4F66

• Entry DOI: 10.2210/pdb4f66/pdb
• Related: 4F79
• Descriptor: Putative phospho-beta-glucosidase, 6-O-phosphono-beta-D-glucopyranose, 1,2-ETHANEDIOL, ... (5 entities in total)
• Functional Keywords: structural genomics, psi-biology, protein structure initiative, midwest center for structural genomics, mcsg, hydrolase
• Biological source: Streptococcus mutans
• Total number of polymer chains: 2
• Total formula weight: 111811.28

Authors

Tan, K.,Michalska, K.,Hatzos-Skintges, C.,Bearden, J.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2012-05-14, release date: 2012-06-13, Last modification date: 2023-09-13)

Primary citation

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. D Biol. Crystallogr., 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

Experimental method

X-RAY DIFFRACTION (1.479 Å)