4gpn

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Current revision (15:52, 14 March 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4gpn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_mutans_UA159 Streptococcus mutans UA159]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GPN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GPN FirstGlance]. <br>
<table><tr><td colspan='2'>[[4gpn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_mutans_UA159 Streptococcus mutans UA159]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GPN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GPN FirstGlance]. <br>
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</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=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PRD_900069:gentiobiose+6-phosphate'>PRD_900069</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.291&#8491;</td></tr>
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<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=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PRD_900069:gentiobiose+6-phosphate'>PRD_900069</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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=4gpn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gpn OCA], [https://pdbe.org/4gpn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gpn RCSB], [https://www.ebi.ac.uk/pdbsum/4gpn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gpn 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=4gpn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gpn OCA], [https://pdbe.org/4gpn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gpn RCSB], [https://www.ebi.ac.uk/pdbsum/4gpn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gpn 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]
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 4gpn" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Beta-glucosidase 3D structures|Beta-glucosidase 3D structures]]
*[[Beta-glucosidase 3D structures|Beta-glucosidase 3D structures]]
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== References ==
 
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<references/>
 
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__TOC__
</StructureSection>
</StructureSection>

Current revision

The crystal structure of 6-P-beta-D-Glucosidase (E375Q mutant) from Streptococcus mutans UA150 in complex with Gentiobiose 6-phosphate.

PDB ID 4gpn

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