5ns6: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Crystal structure of beta-glucosidase BglM-G1 from marine metagenome== | ==Crystal structure of beta-glucosidase BglM-G1 from marine metagenome== | ||
<StructureSection load='5ns6' size='340' side='right' caption='[[5ns6]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='5ns6' size='340' side='right'caption='[[5ns6]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ns6]] is a 3 chain structure. 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 [http:// | <table><tr><td colspan='2'>[[5ns6]] is a 3 chain structure. 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 [http://proteopedia.org/fgij/fg.htm?mol=5NS6 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-glucosidase Beta-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.21 3.2.1.21] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-glucosidase Beta-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.21 3.2.1.21] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5ns6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ns6 OCA], [http://pdbe.org/5ns6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ns6 RCSB], [http://www.ebi.ac.uk/pdbsum/5ns6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ns6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 17: | Line 17: | ||
</div> | </div> | ||
<div class="pdbe-citations 5ns6" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5ns6" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Beta-glucosidase 3D structures|Beta-glucosidase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 22: | Line 25: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Beta-glucosidase]] | [[Category: Beta-glucosidase]] | ||
[[Category: Large Structures]] | |||
[[Category: Gasper, R]] | [[Category: Gasper, R]] | ||
[[Category: Hofmann, E]] | [[Category: Hofmann, E]] | ||
Revision as of 11:27, 4 November 2020
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
|
| ||||||||||||||||||