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| | ==Dehydrogenase domain of Myriococcum thermophilum cellobiose dehydrogenase, MtDH== | | ==Dehydrogenase domain of Myriococcum thermophilum cellobiose dehydrogenase, MtDH== |
| - | <StructureSection load='4qi4' size='340' side='right' caption='[[4qi4]], [[Resolution|resolution]] 2.70Å' scene=''> | + | <StructureSection load='4qi4' size='340' side='right'caption='[[4qi4]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4qi4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_22112 Atcc 22112]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QI4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QI4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4qi4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermothelomyces_myriococcoides Thermothelomyces myriococcoides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QI4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QI4 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 2.7Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qi3|4qi3]], [[4qi5|4qi5]], [[4qi6|4qi6]], [[4qi7|4qi7]], [[4qi8|4qi8]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CDH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=455373 ATCC 22112])</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=4qi4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qi4 OCA], [https://pdbe.org/4qi4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qi4 RCSB], [https://www.ebi.ac.uk/pdbsum/4qi4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qi4 ProSAT]</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=4qi4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qi4 OCA], [http://pdbe.org/4qi4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qi4 RCSB], [http://www.ebi.ac.uk/pdbsum/4qi4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qi4 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A9XK88_9PEZI A9XK88_9PEZI] |
| | <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: Atcc 22112]] | + | [[Category: Large Structures]] |
| - | [[Category: Divne, C]] | + | [[Category: Thermothelomyces myriococcoides]] |
| - | [[Category: Gandini, R]] | + | [[Category: Divne C]] |
| - | [[Category: Hallberg, B M]] | + | [[Category: Gandini R]] |
| - | [[Category: Haltrich, D]] | + | [[Category: Hallberg BM]] |
| - | [[Category: Kittl, R]] | + | [[Category: Haltrich D]] |
| - | [[Category: Ludwig, R]] | + | [[Category: Kittl R]] |
| - | [[Category: Sygmund, C]] | + | [[Category: Ludwig R]] |
| - | [[Category: Tan, T C]] | + | [[Category: Sygmund C]] |
| - | [[Category: Cdh cytochrome domain]]
| + | [[Category: Tan TC]] |
| - | [[Category: Cellobiose oxidizing]]
| + | |
| - | [[Category: Electron transfer]]
| + | |
| - | [[Category: Lignocellulose degradation]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
A9XK88_9PEZI
Publication Abstract from PubMed
A new paradigm for cellulose depolymerization by fungi focuses on an oxidative mechanism involving cellobiose dehydrogenases (CDH) and copper-dependent lytic polysaccharide monooxygenases (LPMO); however, mechanistic studies have been hampered by the lack of structural information regarding CDH. CDH contains a haem-binding cytochrome (CYT) connected via a flexible linker to a flavin-dependent dehydrogenase (DH). Electrons are generated from cellobiose oxidation catalysed by DH and shuttled via CYT to LPMO. Here we present structural analyses that provide a comprehensive picture of CDH conformers, which govern the electron transfer between redox centres. Using structure-based site-directed mutagenesis, rapid kinetics analysis and molecular docking, we demonstrate that flavin-to-haem interdomain electron transfer (IET) is enabled by a haem propionate group and that rapid IET requires a closed CDH state in which the propionate is tightly enfolded by DH. Following haem reduction, CYT reduces LPMO to initiate oxygen activation at the copper centre and subsequent cellulose depolymerization.
Structural basis for cellobiose dehydrogenase action during oxidative cellulose degradation.,Tan TC, Kracher D, Gandini R, Sygmund C, Kittl R, Haltrich D, Hallberg BM, Ludwig R, Divne C Nat Commun. 2015 Jul 7;6:7542. doi: 10.1038/ncomms8542. PMID:26151670[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tan TC, Kracher D, Gandini R, Sygmund C, Kittl R, Haltrich D, Hallberg BM, Ludwig R, Divne C. Structural basis for cellobiose dehydrogenase action during oxidative cellulose degradation. Nat Commun. 2015 Jul 7;6:7542. doi: 10.1038/ncomms8542. PMID:26151670 doi:http://dx.doi.org/10.1038/ncomms8542
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