4oif: Difference between revisions
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==3D structure of Gan42B, a GH42 beta-galactosidase from G.== | ==3D structure of Gan42B, a GH42 beta-galactosidase from G.== | ||
<StructureSection load='4oif' size='340' side='right' caption='[[4oif]], [[Resolution|resolution]] 2.45Å' scene=''> | <StructureSection load='4oif' size='340' side='right' caption='[[4oif]], [[Resolution|resolution]] 2.45Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4oij|4oij]], [[4oik|4oik]], [[4ojy|4ojy]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4oij|4oij]], [[4oik|4oik]], [[4ojy|4ojy]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-galactosidase Beta-galactosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.23 3.2.1.23] </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-galactosidase Beta-galactosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.23 3.2.1.23] </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=4oif FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oif OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oif RCSB], [http://www.ebi.ac.uk/pdbsum/4oif PDBsum]</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=4oif FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oif OCA], [http://pdbe.org/4oif PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4oif RCSB], [http://www.ebi.ac.uk/pdbsum/4oif PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4oif ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4oif" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Galactosidase|Galactosidase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 12:20, 11 August 2016
3D structure of Gan42B, a GH42 beta-galactosidase from G.3D structure of Gan42B, a GH42 beta-galactosidase from G.
Structural highlights
Publication Abstract from PubMedGeobacillus stearothermophilus T-6 is a Gram-positive thermophilic soil bacterium that contains a multi-enzyme system for the utilization of plant cell-wall polysaccharides, including xylan, arabinan and galactan. The bacterium uses a number of endo-acting extracellular enzymes that break down the high-molecular-weight polysaccharides into decorated oligosaccharides. These oligosaccharides enter the cell and are further hydrolyzed into sugar monomers by a set of intracellular glycoside hydrolases. One of these intracellular degrading enzymes is GanB, a glycoside hydrolase family 42 beta-galactosidase capable of hydrolyzing short beta-1,4-galactosaccharides to galactose. GanB and related enzymes therefore play an important part in the hemicellulolytic utilization system of many microorganisms which use plant biomass for growth. The interest in the biochemical characterization and structural analysis of these enzymes stems from their potential biotechnological applications. GanB from G. stearothermophilus T-6 has recently been cloned, overexpressed, purified, biochemically characterized and crystallized in our laboratory as part of its complete structure-function study. The best crystals obtained for this enzyme belong to the primitive orthorhombic space group P2(1)2(1)2(1), with average crystallographic unit-cell parameters of a=71.84, b=181.35, c=196.57 A. Full diffraction data sets to 2.45 and 2.50 A resolution have been collected for both the wild-type enzyme and its E323A nucleophile catalytic mutant, respectively, as measured from flash-cooled crystals at 100 K using synchrotron radiation. These data are currently being used for the full three-dimensional crystal structure determination of GanB. Crystallization and preliminary crystallographic analysis of GanB, a GH42 intracellular beta-galactosidase from Geobacillus stearothermophilus.,Solomon HV, Tabachnikov O, Feinberg H, Govada L, Chayen NE, Shoham Y, Shoham G Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Oct;69(Pt 10):1114-9. doi:, 10.1107/S1744309113023609. Epub 2013 Sep 28. PMID:24100561[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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