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4f66
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4f66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f66 OCA], [http://pdbe.org/4f66 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4f66 RCSB], [http://www.ebi.ac.uk/pdbsum/4f66 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4f66 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4f66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f66 OCA], [http://pdbe.org/4f66 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4f66 RCSB], [http://www.ebi.ac.uk/pdbsum/4f66 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4f66 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:23519420</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4f66" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 08:14, 15 November 2017
The crystal structure of 6-phospho-beta-glucosidase from Streptococcus mutans UA159 in complex with beta-D-glucose-6-phosphate.
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