4f79
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4f79]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_mutans Streptococcus mutans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F79 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F79 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4f79]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_mutans Streptococcus mutans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F79 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F79 FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=P53:2-(HYDROXYMETHYL)PHENYL+6-O-PHOSPHONO-BETA-D-GLUCOPYRANOSIDE'>P53</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.54Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=P53:2-(HYDROXYMETHYL)PHENYL+6-O-PHOSPHONO-BETA-D-GLUCOPYRANOSIDE'>P53</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4f79 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f79 OCA], [https://pdbe.org/4f79 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f79 RCSB], [https://www.ebi.ac.uk/pdbsum/4f79 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f79 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4f79 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f79 OCA], [https://pdbe.org/4f79 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f79 RCSB], [https://www.ebi.ac.uk/pdbsum/4f79 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f79 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/Q8DT00_STRMU Q8DT00_STRMU] | [https://www.uniprot.org/uniprot/Q8DT00_STRMU Q8DT00_STRMU] | ||
| - | <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. | ||
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| - | 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> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4f79" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
The crystal structure of 6-phospho-beta-glucosidase mutant (E375Q) in complex with Salicin 6-phosphate
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