5ns7: Difference between revisions

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 <StructureSection load='5ns7' size='340' side='right' caption='[[5ns7]], [[Resolution|resolution]] 1.54&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5ns7]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NS7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NS7 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5ns7]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Marine_metagenome Marine metagenome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NS7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NS7 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>
 <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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ns7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ns7 OCA], [http://pdbe.org/5ns7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ns7 RCSB], [http://www.ebi.ac.uk/pdbsum/5ns7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ns7 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 5ns7" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>
 [[Category: Beta-glucosidase]]
+[[Category: Marine metagenome]]
 [[Category: Gasper, R]]
 [[Category: Hofmann, E]]
 [[Category: Leichert, L I]]
 [[Category: Lupilova, N]]
-[[Category: Pol, D C]]
+[[Category: Mhaindarkar, D C]]
 [[Category: Hydrolase]]
 [[Category: Metagenome]]