4f66

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

spinqualitylabelsall models 4f66, resolution 1.48Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4f66 is a 2 chain structure with sequence from Streptococcus mutans. This structure supersedes the now removed PDB entry 4dde. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BG6, EDO, FMT Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8DT00_STRMU Publication Abstract from PubMed 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 beta-glycosidic bond in 6'-P-beta-glucoside is cleaved, releasing 6-P-beta-glucose and the respective aglycon. This reaction is catalyzed by 6-P-beta-glucosidases, which belong to two glycoside hydrolase (GH) families: GH1 and GH4. Here, the high-resolution crystal structures of GH1 6-P-beta-glucosidases from Lactobacillus plantarum (LpPbg1) and Streptococcus mutans (SmBgl) and their complexes with ligands are reported. Both enzymes show hydrolytic activity towards 6'-P-beta-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-beta-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. GH1-family 6-P-beta-glucosidases from human microbiome lactic acid bacteria.,Michalska K, Tan K, Li H, Hatzos-Skintges C, Bearden J, Babnigg G, Joachimiak A Acta Crystallogr D Biol Crystallogr. 2013 Mar;69(Pt 3):451-63. doi:, 10.1107/S0907444912049608. Epub 2013 Feb 16. PMID:23519420 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA