3ogs: Difference between revisions
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==Complex structure of beta-galactosidase from Trichoderma reesei with IPTG== | ==Complex structure of beta-galactosidase from Trichoderma reesei with IPTG== | ||
<StructureSection load='3ogs' size='340' side='right' caption='[[3ogs]], [[Resolution|resolution]] 1.75Å' scene=''> | <StructureSection load='3ogs' size='340' side='right' caption='[[3ogs]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3og2|3og2]], [[3ogr|3ogr]], [[3ogv|3ogv]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3og2|3og2]], [[3ogr|3ogr]], [[3ogv|3ogv]]</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=3ogs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ogs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ogs RCSB], [http://www.ebi.ac.uk/pdbsum/3ogs 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=3ogs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ogs OCA], [http://pdbe.org/3ogs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ogs RCSB], [http://www.ebi.ac.uk/pdbsum/3ogs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ogs 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 3ogs" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
Revision as of 06:55, 10 December 2016
Complex structure of beta-galactosidase from Trichoderma reesei with IPTGComplex structure of beta-galactosidase from Trichoderma reesei with IPTG
Structural highlights
Publication Abstract from PubMedWe have determined the crystal structure of Trichoderma reesei (Hypocrea jecorina) beta-galactosidase (Tr-beta-gal) at a 1.2A resolution and its complex structures with galactose, IPTG and PETG at 1.5, 1.75 and 1.4A resolutions, respectively. Tr-beta-gal is a potential enzyme for lactose hydrolysis in the dairy industry and belongs to family 35 of the glycoside hydrolases (GH-35). The high resolution crystal structures of this six-domain enzyme revealed interesting features about the structure of Tr-beta-gal. We discovered conformational changes in the two loop regions in the active site, implicating a conformational selection-mechanism for the enzyme. In addition, the Glu200, an acid/base catalyst showed two different conformations which undoubtedly affect the pK(a) value of this residue and the catalytic mechanism. The electron density showed extensive glycosylation, suggesting a structure stabilizing role for glycans. The longest glycan showed an electron density that extends to the eighth monosaccharide unit in the extended chain. The Tr-beta-gal structure also showed a well-ordered structure for a unique octaserine motif on the surface loop of the fifth domain. Crystal structures of Trichoderma reesei beta-galactosidase reveal conformational changes in the active site.,Maksimainen M, Hakulinen N, Kallio JM, Timoharju T, Turunen O, Rouvinen J J Struct Biol. 2011 Apr;174(1):156-63. Epub 2010 Dec 3. PMID:21130883[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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