3QOM
Crystal structure of 6-phospho-beta-glucosidase from Lactobacillus plantarum
Summary for 3QOM
| Entry DOI | 10.2210/pdb3qom/pdb |
| Descriptor | 6-phospho-beta-glucosidase, beta-D-glucopyranose, PHOSPHATE ION, ... (5 entities in total) |
| Functional Keywords | structural genomics, psi-biology, midwest center for structural genomics, mcsg, glycoside hydrolase, hydrolase |
| Biological source | Lactobacillus plantarum |
| Total number of polymer chains | 1 |
| Total formula weight | 56424.48 |
| Authors | Michalska, K.,Hatzos-Skintges, C.,Bearden, J.,Kohler, M.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2011-02-10, release date: 2011-03-09, Last modification date: 2024-10-16) |
| 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.,Sect.D, 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: 23519420DOI: 10.1107/S0907444912049608 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.498 Å) |
Structure validation
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