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| | ==Solvent-stable cholesterol oxidase== | | ==Solvent-stable cholesterol oxidase== |
| - | <StructureSection load='3js8' size='340' side='right' caption='[[3js8]], [[Resolution|resolution]] 1.54Å' scene=''> | + | <StructureSection load='3js8' size='340' side='right'caption='[[3js8]], [[Resolution|resolution]] 1.54Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3js8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chromobacterium_sp._ds-1 Chromobacterium sp. ds-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JS8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3JS8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3js8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chromobacterium_sp._DS-1 Chromobacterium sp. DS-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JS8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JS8 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SUC:SUCROSE'>SUC</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]] 1.54Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1i19|1i19]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FRU:FRUCTOSE'>FRU</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900003:sucrose'>PRD_900003</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cho ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=507619 Chromobacterium sp. DS-1])</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=3js8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3js8 OCA], [https://pdbe.org/3js8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3js8 RCSB], [https://www.ebi.ac.uk/pdbsum/3js8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3js8 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cholesterol_oxidase Cholesterol oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.6 1.1.3.6] </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=3js8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3js8 OCA], [http://pdbe.org/3js8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3js8 RCSB], [http://www.ebi.ac.uk/pdbsum/3js8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3js8 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/B5MGF8_9NEIS B5MGF8_9NEIS] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cholesterol oxidase]] | + | [[Category: Chromobacterium sp. DS-1]] |
| - | [[Category: Chromobacterium sp. ds-1]] | + | [[Category: Large Structures]] |
| - | [[Category: Doukyu, N]] | + | [[Category: Doukyu N]] |
| - | [[Category: Newton, K]] | + | [[Category: Newton K]] |
| - | [[Category: Ohtaki, A]] | + | [[Category: Ohtaki A]] |
| - | [[Category: Sagermann, M]] | + | [[Category: Sagermann M]] |
| - | [[Category: Cholsterol]]
| + | |
| - | [[Category: Fad]]
| + | |
| - | [[Category: Flavoprotein]]
| + | |
| - | [[Category: Organic solvent stability]]
| + | |
| - | [[Category: Oxidase]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Oxygen channel]]
| + | |
| Structural highlights
Function
B5MGF8_9NEIS
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
Cholesterol oxidase is of significant commercial interest as it is widely used as a biosensor for the detection of cholesterol in clinical samples, blood serum and food. Increased stability of this enzyme with regards to temperature and different solvent conditions are of great importance to the reliability and versatility of its applications. We here report the crystal structure of the cholesterol oxidase of Chromobacterium sp. DS-1 (CHOLOX). In contrast to other previously characterized cholesterol oxidases, this enzyme retains high activity in organic solvents and detergents at temperatures above 85 degrees C despite its mesophilic origin. With the availability of one other homologous oxidase of known three-dimensional structure, a detailed comparison of its sequence and structure was performed to elucidate the mechanisms of stabilization. In contrast to factors that typically contribute to the stability of thermophilic proteins, the structure of CHOLOX exhibits a larger overall cavity volume, less charged residues and less salt bridge interactions. Moreover, the vast majority of residue substitutions were found on or near the protein's solvent exposed surface. We propose that the engineering of enhanced stability may also be accomplished through selective engineering of the protein periphery rather than by redesigning its entire core.
Structural characterization of the organic solvent-stable cholesterol oxidase from Chromobacterium sp. DS-1.,Sagermann M, Ohtaki A, Newton K, Doukyu N J Struct Biol. 2010 Apr;170(1):32-40. Epub 2010 Jan 25. PMID:20102741[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sagermann M, Ohtaki A, Newton K, Doukyu N. Structural characterization of the organic solvent-stable cholesterol oxidase from Chromobacterium sp. DS-1. J Struct Biol. 2010 Apr;170(1):32-40. Epub 2010 Jan 25. PMID:20102741 doi:10.1016/j.jsb.2010.01.012
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