5ns6: Difference between revisions
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==Crystal structure of beta-glucosidase BglM-G1 from marine metagenome== | |||
<StructureSection load='5ns6' size='340' side='right'caption='[[5ns6]], [[Resolution|resolution]] 1.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5ns6]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Marine_metagenome Marine metagenome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NS6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NS6 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</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=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=5ns6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ns6 OCA], [https://pdbe.org/5ns6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ns6 RCSB], [https://www.ebi.ac.uk/pdbsum/5ns6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ns6 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Salt bridges are the strongest electrostatic interactions in proteins. They substantially contribute to a protein's structural stability. Thus, mutations of salt bridges are typically selected against. Here, we report on the evolutionary loss of a highly conserved salt bridge in the GH1 family glycosyl hydrolase BglM-G1. BglM-G1's gene was found in the bacterial metagenome of a temperate, seasonally cold marine habitat. In BglM-G1, arginine 75 is replaced by a histidine. While fully retaining beta-glucosidase activity, BglM-G1 is less heat stable than an H75R variant, in which the salt bridge was artificially re-introduced. However, the K m toward its substrates was lower in wild type, leading to an overall higher catalytic efficiency. Our results indicate that this loss of the salt bridge leads to higher flexibility in BglM-G1's active site, trading structural stability at high temperatures, a trait not needed in a temperate, seasonally cold habitat, for a more effective catalytic activity. | |||
Loss of a conserved salt bridge in bacterial glycosyl hydrolase BgIM-G1 improves substrate binding in temperate environments.,Mhaindarkar D, Gasper R, Lupilov N, Hofmann E, Leichert LI Commun Biol. 2018 Oct 17;1:171. doi: 10.1038/s42003-018-0167-7. eCollection 2018. PMID:30345395<ref>PMID:30345395</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5ns6" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
[[Category: | *[[Beta-glucosidase 3D structures|Beta-glucosidase 3D structures]] | ||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Marine metagenome]] | |||
[[Category: Gasper R]] | |||
[[Category: Hofmann E]] | |||
[[Category: Leichert LI]] | |||
[[Category: Lupilova N]] | |||
[[Category: Mhaindarkar DC]] | |||
Latest revision as of 15:05, 22 November 2023
Crystal structure of beta-glucosidase BglM-G1 from marine metagenomeCrystal structure of beta-glucosidase BglM-G1 from marine metagenome
Structural highlights
Publication Abstract from PubMedSalt bridges are the strongest electrostatic interactions in proteins. They substantially contribute to a protein's structural stability. Thus, mutations of salt bridges are typically selected against. Here, we report on the evolutionary loss of a highly conserved salt bridge in the GH1 family glycosyl hydrolase BglM-G1. BglM-G1's gene was found in the bacterial metagenome of a temperate, seasonally cold marine habitat. In BglM-G1, arginine 75 is replaced by a histidine. While fully retaining beta-glucosidase activity, BglM-G1 is less heat stable than an H75R variant, in which the salt bridge was artificially re-introduced. However, the K m toward its substrates was lower in wild type, leading to an overall higher catalytic efficiency. Our results indicate that this loss of the salt bridge leads to higher flexibility in BglM-G1's active site, trading structural stability at high temperatures, a trait not needed in a temperate, seasonally cold habitat, for a more effective catalytic activity. Loss of a conserved salt bridge in bacterial glycosyl hydrolase BgIM-G1 improves substrate binding in temperate environments.,Mhaindarkar D, Gasper R, Lupilov N, Hofmann E, Leichert LI Commun Biol. 2018 Oct 17;1:171. doi: 10.1038/s42003-018-0167-7. eCollection 2018. PMID:30345395[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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