3ogs: Difference between revisions
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==Complex structure of beta-galactosidase from Trichoderma reesei with IPTG== | |||
<StructureSection load='3ogs' size='340' side='right'caption='[[3ogs]], [[Resolution|resolution]] 1.75Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3ogs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichoderma_reesei Trichoderma reesei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OGS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OGS 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]] 1.75Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=IPT:ISOPROPYL-1-BETA-D-THIOGALACTOSIDE'>IPT</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=3ogs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ogs OCA], [https://pdbe.org/3ogs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ogs RCSB], [https://www.ebi.ac.uk/pdbsum/3ogs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ogs ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q70SY0_HYPJE Q70SY0_HYPJE] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
We 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<ref>PMID:21130883</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3ogs" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Galactosidase|Galactosidase]] | *[[Galactosidase 3D structures|Galactosidase 3D structures]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Trichoderma reesei]] | [[Category: Trichoderma reesei]] | ||
[[Category: Maksimainen | [[Category: Maksimainen M]] | ||
[[Category: Rouvinen | [[Category: Rouvinen J]] | ||
Latest revision as of 19:55, 1 November 2023
Complex structure of beta-galactosidase from Trichoderma reesei with IPTGComplex structure of beta-galactosidase from Trichoderma reesei with IPTG
Structural highlights
FunctionPublication 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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