7p38

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Current revision (07:52, 1 May 2024) (edit) (undo)
 
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<StructureSection load='7p38' size='340' side='right'caption='[[7p38]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='7p38' size='340' side='right'caption='[[7p38]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7p38]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7P38 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7P38 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[7p38]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Limosilactobacillus_reuteri Limosilactobacillus reuteri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7P38 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7P38 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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.7&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Dextransucrase Dextransucrase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.5 2.4.1.5] </span></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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=7p38 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7p38 OCA], [https://pdbe.org/7p38 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7p38 RCSB], [https://www.ebi.ac.uk/pdbsum/7p38 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7p38 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=7p38 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7p38 OCA], [https://pdbe.org/7p38 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7p38 RCSB], [https://www.ebi.ac.uk/pdbsum/7p38 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7p38 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/A0A1Z2RUH3_LACRE A0A1Z2RUH3_LACRE]] Production of extracellular glucans, that are thought to play a key role in the development of the dental plaque because of their ability to adhere to smooth surfaces and mediate the aggregation of bacterial cells and food debris.[ARBA:ARBA00003243]
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[https://www.uniprot.org/uniprot/A0A1Z2RUH3_LIMRT A0A1Z2RUH3_LIMRT] Production of extracellular glucans, that are thought to play a key role in the development of the dental plaque because of their ability to adhere to smooth surfaces and mediate the aggregation of bacterial cells and food debris.[ARBA:ARBA00003243]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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GtfB-type alpha-glucanotransferase enzymes from glycoside hydrolase family 70 (GH70) convert starch substrates into alpha-glucans that are of interest as food ingredients with a low glycemic index. Characterization of several GtfBs showed that they differ in product- and substrate specificity, especially with regard to branching, but structural information is limited to a single GtfB, preferring mostly linear starches and featuring a tunneled binding groove. Here, we present the second crystal structure of a 4,6-alpha-glucanotransferase (Limosilactobacillus reuteri NCC 2613) and an improved homology model of a 4,3-alpha-glucanotransferase GtfB (L. fermentum NCC 2970) and show that they are able to convert both linear and branched starch substrates. Compared to the previously described GtfB structure, these two enzymes feature a much more open binding groove, reminiscent of and evolutionary closer to starch-converting GH13 alpha-amylases. Sequence analysis of 287 putative GtfBs suggests that only 20% of them are similarly "open" and thus suitable as broad-specificity starch-converting enzymes.
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Insights into Broad-Specificity Starch Modification from the Crystal Structure of Limosilactobacillus Reuteri NCC 2613 4,6-alpha-Glucanotransferase GtfB.,Pijning T, Gangoiti J, Te Poele EM, Borner T, Dijkhuizen L J Agric Food Chem. 2021 Oct 28. doi: 10.1021/acs.jafc.1c05657. PMID:34708648<ref>PMID:34708648</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 7p38" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Dextransucrase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Boerner, T]]
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[[Category: Limosilactobacillus reuteri]]
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[[Category: Dijkhuizen, L]]
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[[Category: Boerner T]]
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[[Category: Gangoiti, J]]
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[[Category: Dijkhuizen L]]
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[[Category: Pijning, T]]
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[[Category: Gangoiti J]]
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[[Category: Poele, E te]]
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[[Category: Pijning T]]
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[[Category: 6-alpha-transglycosylation]]
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[[Category: Te Poele E]]
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[[Category: Gtfb]]
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[[Category: Starch conversion]]
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[[Category: Transferase]]
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Current revision

4,6-alpha-glucanotransferase GtfB from Limosilactobacillus reuteri NCC 2613

PDB ID 7p38

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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