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4F79

The crystal structure of 6-phospho-beta-glucosidase mutant (E375Q) in complex with Salicin 6-phosphate

Summary for 4F79
Entry DOI10.2210/pdb4f79/pdb
Related3PN8 4F66
DescriptorPutative phospho-beta-glucosidase, 2-(hydroxymethyl)phenyl 6-O-phosphono-beta-D-glucopyranoside, GLYCEROL, ... (4 entities in total)
Functional Keywordsstructural genomics, psi-biology, protein structure initiative, midwest center for structural genomics, mcsg, hydrolase
Biological sourceStreptococcus mutans
Total number of polymer chains1
Total formula weight56024.81
Authors
Tan, K.,Michalska, K.,Li, H.,Jedrzejczak, R.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2012-05-15, release date: 2012-06-13, Last modification date: 2023-09-13)
Primary citationMichalska, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.54 Å)
Structure validation

238582

数据于2025-07-09公开中

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