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4c7x

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<StructureSection load='4c7x' size='340' side='right'caption='[[4c7x]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
<StructureSection load='4c7x' size='340' side='right'caption='[[4c7x]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4c7x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lacs1 Lacs1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C7X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C7X FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4c7x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ligilactobacillus_salivarius_UCC118 Ligilactobacillus salivarius UCC118]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C7X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C7X FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr>
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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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4c7v|4c7v]]</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4c7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c7x OCA], [https://pdbe.org/4c7x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c7x RCSB], [https://www.ebi.ac.uk/pdbsum/4c7x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c7x ProSAT]</span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transketolase Transketolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.2.1.1 2.2.1.1] </span></td></tr>
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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=4c7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c7x OCA], [http://pdbe.org/4c7x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c7x RCSB], [http://www.ebi.ac.uk/pdbsum/4c7x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c7x ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[[https://www.uniprot.org/uniprot/Q1WQU8_LIGS1 Q1WQU8_LIGS1]]
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Probiotic bacterial strains have been shown to enhance the health of the host through a range of mechanisms including colonization, resistance against pathogens, secretion of antimicrobial compounds and modulation of the activity of the innate immune system. Lactobacillus salivarius UCC118 is a well characterized probiotic strain which survives intestinal transit and has many desirable host-interaction properties. Probiotic bacteria display a wide range of catabolic activities, which determine their competitiveness in vivo. Some lactobacilli are heterofermentative and can metabolize pentoses, using a pathway in which transketolase and transaldolase are key enzymes. L. salivarius UCC118 is capable of pentose utilization because it encodes the key enzymes on a megaplasmid. The crystal structures of the megaplasmid-encoded transketolase with and without the enzyme cofactor thiamine pyrophosphate have been determined. Comparisons with other known transketolase structures reveal a high degree of structural conservation in both the catalytic site and the overall conformation. This work extends structural knowledge of the transketolases to the industrially and commercially important Lactobacillus genus.
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High-resolution structures of Lactobacillus salivarius transketolase in the presence and absence of thiamine pyrophosphate.,Lukacik P, Lobley CM, Bumann M, Arena de Souza V, Owens RJ, O'Toole PW, Walsh MA Acta Crystallogr F Struct Biol Commun. 2015 Oct 1;71(Pt 10):1327-34. doi:, 10.1107/S2053230X1501657X. Epub 2015 Sep 23. PMID:26457526<ref>PMID:26457526</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 4c7x" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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*[[Transketolase|Transketolase]]
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*[[Transketolase 3D structures|Transketolase 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Lacs1]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Transketolase]]
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[[Category: Ligilactobacillus salivarius UCC118]]
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[[Category: Aller, P]]
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[[Category: Aller P]]
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[[Category: Bumann, M]]
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[[Category: Bumann M]]
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[[Category: Douangamath, A]]
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[[Category: Douangamath A]]
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[[Category: Lobley, C M.C]]
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[[Category: Lobley CMC]]
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[[Category: Lukacik, P]]
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[[Category: Lukacik P]]
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[[Category: Toole, P W.O]]
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[[Category: O'Toole PW]]
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[[Category: Walsh, M A]]
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[[Category: Walsh MA]]
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[[Category: Transferase]]
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Revision as of 17:31, 7 September 2022

Thiamine Pyrophosphate Bound Transketolase from Lactobacillus salivarius at 2.2A resolution

PDB ID 4c7x

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