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| | ==The crystal structure of 6-phospho-beta-glucosidase from Streptococcus mutans UA159 in complex with beta-D-glucose-6-phosphate.== | | ==The crystal structure of 6-phospho-beta-glucosidase from Streptococcus mutans UA159 in complex with beta-D-glucose-6-phosphate.== |
| - | <StructureSection load='4f66' size='340' side='right' caption='[[4f66]], [[Resolution|resolution]] 1.48Å' scene=''> | + | <StructureSection load='4f66' size='340' side='right'caption='[[4f66]], [[Resolution|resolution]] 1.48Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4f66]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_25175 Atcc 25175]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4dde 4dde]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F66 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F66 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4f66]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_mutans Streptococcus mutans]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4dde 4dde]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F66 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F66 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BG6:BETA-D-GLUCOSE-6-PHOSPHATE'>BG6</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BG6:BETA-D-GLUCOSE-6-PHOSPHATE'>BG6</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4f79|4f79]]</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=4f66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f66 OCA], [https://pdbe.org/4f66 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f66 RCSB], [https://www.ebi.ac.uk/pdbsum/4f66 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f66 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bgl, SMU_1601 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1309 ATCC 25175])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/6-phospho-beta-glucosidase 6-phospho-beta-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.86 3.2.1.86] </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> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8DT00_STRMU Q8DT00_STRMU] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 6-phospho-beta-glucosidase]] | + | [[Category: Large Structures]] |
| - | [[Category: Atcc 25175]] | + | [[Category: Streptococcus mutans]] |
| - | [[Category: Bearden, J]] | + | [[Category: Bearden J]] |
| - | [[Category: Hatzos-Skintges, C]] | + | [[Category: Hatzos-Skintges C]] |
| - | [[Category: Joachimiak, A]] | + | [[Category: Joachimiak A]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Michalska K]] |
| - | [[Category: Michalska, K]] | + | [[Category: Tan K]] |
| - | [[Category: Tan, K]] | + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Mcsg]]
| + | |
| - | [[Category: PSI, Protein structure initiative]]
| + | |
| - | [[Category: Psi-biology]]
| + | |
| Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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 D Biol Crystallogr. 2013 Mar;69(Pt 3):451-63. doi:, 10.1107/S0907444912049608. Epub 2013 Feb 16. PMID:23519420 doi:http://dx.doi.org/10.1107/S0907444912049608
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