3ahy

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{{Seed}}
 
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[[Image:3ahy.png|left|200px]]
 
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==Crystal structure of beta-glucosidase 2 from fungus Trichoderma reesei in complex with Tris==
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The line below this paragraph, containing "STRUCTURE_3ahy", creates the "Structure Box" on the page.
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<StructureSection load='3ahy' size='340' side='right'caption='[[3ahy]], [[Resolution|resolution]] 1.63&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3ahy]] is a 4 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=3AHY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AHY FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.63&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
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{{STRUCTURE_3ahy| PDB=3ahy | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ahy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ahy OCA], [https://pdbe.org/3ahy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ahy RCSB], [https://www.ebi.ac.uk/pdbsum/3ahy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ahy ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/O93785_HYPJE O93785_HYPJE]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ah/3ahy_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3ahy ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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beta-Glucosidases (EC 3.2.1.21) cleave beta-glucosidic linkages in disaccharide or glucose-substituted molecules and play important roles in fundamental biological processes. beta-Glucosidases have been widely used in agricultural, biotechnological, industrial and medical applications. In this study, a high yield expression (70-250mg/l) in Escherichia coli of the three functional beta-glucosidase genes was obtained from the bacterium Clostridium cellulovorans (CcBglA), the fungus Trichoderma reesei (TrBgl2), and the termite Neotermes koshunensis (NkBgl) with the crystal structures of CcBglA, TrBgl2 and NkBgl, determined at 1.9A, 1.63A and 1.34A resolution, respectively. The overall structures of these enzymes are similar to those belonging to the beta-retaining glycosyl hydrolase family 1, which have a classical (alpha/beta)(8)-TIM barrel fold. Each contains a slot-like active site cleft and a more variable outer opening, related to its function in processing different lengths of beta-1,4-linked glucose derivatives. The two essential glutamate residues for hydrolysis are spatially conserved in the active site. In both TrBgl2 and NkBgl structures, a Tris molecule was found to bind at the active site, explaining the slight inhibition of hydrolase activity observed in Tris buffer. Manganese ions at 10mM exerted an approximate 2-fold enzyme activity enhancement of all three beta-glucosidases, with CcBglA catalyzing the most efficiently in hydrolysis reaction and tolerating Tris as well as some metal inhibition. In summary, our results for the structural and functional properties of these three beta-glucosidases from various biological sources open important avenues of exploration for further practical applications.
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===Crystal structure of beta-glucosidase 2 from fungus Trichoderma reesei in complex with Tris===
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Structural and functional analysis of three beta-glucosidases from bacterium Clostridium cellulovorans, fungus Trichoderma reesei and termite Neotermes koshunensis.,Jeng WY, Wang NC, Lin MH, Lin CT, Liaw YC, Chang WJ, Liu CI, Liang PH, Wang AH J Struct Biol. 2010 Aug 1. PMID:20682343<ref>PMID:20682343</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3ahy" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_20682343}}, adds the Publication Abstract to the page
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*[[Beta-glucosidase 3D structures|Beta-glucosidase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 20682343 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_20682343}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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3AHY is a 4 chains structure with sequences from [http://en.wikipedia.org/wiki/Hypocrea_jecorina Hypocrea jecorina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AHY OCA].
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[[Category: Trichoderma reesei]]
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[[Category: Jeng W-Y]]
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==Reference==
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[[Category: Liu C-I]]
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<ref group="xtra">PMID:20682343</ref><references group="xtra"/>
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[[Category: Wang AH-J]]
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[[Category: Beta-glucosidase]]
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[[Category: Hypocrea jecorina]]
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[[Category: Jeng, W Y.]]
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[[Category: Liu, C I.]]
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[[Category: Wang, A H.J.]]
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[[Category: Cellulase]]
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[[Category: Glycosyl hydrolase]]
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[[Category: Hydrolase]]
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[[Category: Manganese enhancement]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 22 09:22:24 2010''
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Current revision

Crystal structure of beta-glucosidase 2 from fungus Trichoderma reesei in complex with Tris

PDB ID 3ahy

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