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| | <StructureSection load='1olr' size='340' side='right'caption='[[1olr]], [[Resolution|resolution]] 1.20Å' scene=''> | | <StructureSection load='1olr' size='340' side='right'caption='[[1olr]], [[Resolution|resolution]] 1.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1olr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Humicola_grisea Humicola grisea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OLR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OLR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1olr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichocladium_griseum Trichocladium griseum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OLR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OLR FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.2Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></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=1olr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1olr OCA], [http://pdbe.org/1olr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1olr RCSB], [http://www.ebi.ac.uk/pdbsum/1olr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1olr ProSAT]</span></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=1olr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1olr OCA], [https://pdbe.org/1olr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1olr RCSB], [https://www.ebi.ac.uk/pdbsum/1olr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1olr ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8NJY3_9PEZI Q8NJY3_9PEZI] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ol/1olr_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ol/1olr_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cellulase]] | |
| - | [[Category: Humicola grisea]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Berglund, G I]] | + | [[Category: Trichocladium griseum]] |
| - | [[Category: Gross, L S]] | + | [[Category: Berglund GI]] |
| - | [[Category: Gualfetti, P J]] | + | [[Category: Gross LS]] |
| - | [[Category: Jones, T A]] | + | [[Category: Gualfetti PJ]] |
| - | [[Category: Mitchinson, C]] | + | [[Category: Jones TA]] |
| - | [[Category: Saldajeno, M]] | + | [[Category: Mitchinson C]] |
| - | [[Category: Sandgren, M]] | + | [[Category: Saldajeno M]] |
| - | [[Category: Shaw, A]] | + | [[Category: Sandgren M]] |
| - | [[Category: Cellulose degradation]]
| + | [[Category: Shaw A]] |
| - | [[Category: Endoglucanase]]
| + | |
| - | [[Category: Gh family 12]]
| + | |
| - | [[Category: Glycosyl hydrolase]]
| + | |
| - | [[Category: Humicola grisea cel12a]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
Q8NJY3_9PEZI
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
As part of a program to discover improved glycoside hydrolase family 12 (GH 12) endoglucanases, we have extended our previous work on the structural and biochemical diversity of GH 12 homologs to include the most stable fungal GH 12 found, Humicola grisea Cel12A. The H. grisea enzyme was much more stable to irreversible thermal denaturation than the Trichoderma reesei enzyme. It had an apparent denaturation midpoint (T(m)) of 68.7 degrees C, 14.3 degrees C higher than the T. reesei enzyme. There are an additional three cysteines found in the H. grisea Cel12A enzyme. To determine their importance for thermal stability, we constructed three H. grisea Cel12A single mutants in which these cysteines were exchanged with the corresponding residues in the T. reesei enzyme. We also introduced these cysteine residues into the T. reesei enzyme. The thermal stability of these variants was determined. Substitutions at any of the three positions affected stability, with the largest effect seen in H. grisea C206P, which has a T(m) 9.1 degrees C lower than that of the wild type. The T. reesei cysteine variant that gave the largest increase in stability, with a T(m) 3.9 degrees C higher than wild type, was the P201C mutation, the converse of the destabilizing C206P mutation in H. grisea. To help rationalize the results, we have determined the crystal structure of the H. grisea enzyme and of the most stable T. reesei cysteine variant, P201C. The three cysteines in H. grisea Cel12A play an important role in the thermal stability of this protein, although they are not involved in a disulfide bond.
The Humicola grisea Cel12A enzyme structure at 1.2 A resolution and the impact of its free cysteine residues on thermal stability.,Sandgren M, Gualfetti PJ, Paech C, Paech S, Shaw A, Gross LS, Saldajeno M, Berglund GI, Jones TA, Mitchinson C Protein Sci. 2003 Dec;12(12):2782-93. PMID:14627738[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sandgren M, Gualfetti PJ, Paech C, Paech S, Shaw A, Gross LS, Saldajeno M, Berglund GI, Jones TA, Mitchinson C. The Humicola grisea Cel12A enzyme structure at 1.2 A resolution and the impact of its free cysteine residues on thermal stability. Protein Sci. 2003 Dec;12(12):2782-93. PMID:14627738
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