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| | <StructureSection load='6qzo' size='340' side='right'caption='[[6qzo]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='6qzo' size='340' side='right'caption='[[6qzo]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6qzo]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Cellulomonas_bogoriensis_69b4 Cellulomonas bogoriensis 69b4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QZO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QZO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6qzo]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Cellulomonas_bogoriensis_69B4_=_DSM_16987 Cellulomonas bogoriensis 69B4 = DSM 16987]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QZO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QZO FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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]] 2.4Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">N869_13850 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1386082 Cellulomonas bogoriensis 69B4])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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=6qzo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qzo OCA], [http://pdbe.org/6qzo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qzo RCSB], [http://www.ebi.ac.uk/pdbsum/6qzo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qzo 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=6qzo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qzo OCA], [https://pdbe.org/6qzo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qzo RCSB], [https://www.ebi.ac.uk/pdbsum/6qzo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qzo ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A0A0BZU2_9CELL A0A0A0BZU2_9CELL] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cellulomonas bogoriensis 69b4]] | + | [[Category: Cellulomonas bogoriensis 69B4 = DSM 16987]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Fraaije, M W]] | + | [[Category: Fraaije MW]] |
| - | [[Category: Rozeboom, H J]] | + | [[Category: Rozeboom HJ]] |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
A0A0A0BZU2_9CELL
Publication Abstract from PubMed
DyP-type peroxidases are heme-containing enzymes that have received increasing attention over recent years with regards to their potential as biocatalysts. A novel DyP-type peroxidase (CboDyP) was discovered from the alkaliphilic cellulomonad, Cellulomonas bogoriensis, which could be overexpressed in Escherichia coli. The biochemical characterization of the recombinant enzyme showed that it is a heme-containing enzyme capable to act as a peroxidase on several dyes. With the tested substrates, the enzyme is most active at acidic pH values and is quite tolerant towards solvents. The crystal structure of CboDyP was solved which revealed atomic details of the dimeric heme-containing enzyme. A peculiar feature of CboDyP is the presence of a glutamate in the active site which in most other DyPs is an aspartate, being part of the DyP-typifying sequence motif GXXDG. The E201D CboDyP mutant was prepared and analyzed which revealed that the mutant enzyme shows a significantly higher activity on several dyes when compared with the wild-type enzyme.
Characterization of a New DyP-Peroxidase from the Alkaliphilic Cellulomonad, Cellulomonas bogoriensis.,Habib MH, Rozeboom HJ, Fraaije MW Molecules. 2019 Mar 27;24(7). pii: molecules24071208. doi:, 10.3390/molecules24071208. PMID:30934796[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Habib MH, Rozeboom HJ, Fraaije MW. Characterization of a New DyP-Peroxidase from the Alkaliphilic Cellulomonad, Cellulomonas bogoriensis. Molecules. 2019 Mar 27;24(7). pii: molecules24071208. doi:, 10.3390/molecules24071208. PMID:30934796 doi:http://dx.doi.org/10.3390/molecules24071208
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